HEADER SIGNALING PROTEIN 15-AUG-16 5T04 TITLE STRUCTURE OF CONSTITUTIVELY ACTIVE NEUROTENSIN RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROTENSIN RECEPTOR TYPE 1,ENDOLYSIN,NEUROTENSIN RECEPTOR COMPND 3 TYPE 1; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP RESIDUES 43-268; 2-161; 297-396,UNP RESIDUES 43-268; 2- COMPND 6 161; 297-396,UNP RESIDUES 43-268; 2-161; 297-396; COMPND 7 SYNONYM: NTR1,HIGH-AFFINITY LEVOCABASTINE-INSENSITIVE NEUROTENSIN COMPND 8 RECEPTOR,NTRH,LYSIS PROTEIN,LYSOZYME,MURAMIDASE,NTR1,HIGH-AFFINITY COMPND 9 LEVOCABASTINE-INSENSITIVE NEUROTENSIN RECEPTOR,NTRH; COMPND 10 EC: 3.2.1.17; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES; COMPND 13 MOL_ID: 2; COMPND 14 MOLECULE: ARG-ARG-PRO-TYR-ILE-LEU; COMPND 15 CHAIN: B; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: RAT; SOURCE 4 ORGANISM_TAXID: 10116, 10665; SOURCE 5 GENE: NTSR1, NTSR; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: CABBAGE LOOPER; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1; SOURCE 12 MOL_ID: 2; SOURCE 13 SYNTHETIC: YES; SOURCE 14 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 15 ORGANISM_TAXID: 10116 KEYWDS MEMBRANE PROTEIN, G PROTEIN-COUPLED RECEPTOR, GPCR, NEUROTENSIN KEYWDS 2 RECEPTOR, NTSR1, SIGNALING PROTEIN, AGONIST EXPDTA X-RAY DIFFRACTION AUTHOR B.KRUMM,I.BOTOS,R.GRISSHAMMER REVDAT 1 21-DEC-16 5T04 0 JRNL AUTH B.E.KRUMM,S.LEE,S.BHATTACHARYA,I.BOTOS,C.F.WHITE,H.DU, JRNL AUTH 2 N.VAIDEHI,R.GRISSHAMMER JRNL TITL STRUCTURE AND DYNAMICS OF A CONSTITUTIVELY ACTIVE JRNL TITL 2 NEUROTENSIN RECEPTOR. JRNL REF SCI REP V. 6 38564 2016 JRNL REFN ESSN 2045-2322 JRNL PMID 27924846 JRNL DOI 10.1038/SREP38564 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10_2155: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.14 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 18582 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.256 REMARK 3 R VALUE (WORKING SET) : 0.253 REMARK 3 FREE R VALUE : 0.283 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.990 REMARK 3 FREE R VALUE TEST SET COUNT : 1484 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 38.1439 - 7.3241 0.99 1588 149 0.1883 0.1754 REMARK 3 2 7.3241 - 5.8200 1.00 1594 141 0.2531 0.2850 REMARK 3 3 5.8200 - 5.0863 1.00 1635 99 0.2682 0.3767 REMARK 3 4 5.0863 - 4.6221 1.00 1574 157 0.2461 0.2910 REMARK 3 5 4.6221 - 4.2913 1.00 1571 147 0.2497 0.3159 REMARK 3 6 4.2913 - 4.0386 1.00 1607 124 0.2568 0.2978 REMARK 3 7 4.0386 - 3.8365 1.00 1594 153 0.2814 0.3394 REMARK 3 8 3.8365 - 3.6696 1.00 1596 136 0.2973 0.3427 REMARK 3 9 3.6696 - 3.5285 0.99 1610 126 0.3067 0.2943 REMARK 3 10 3.5285 - 3.4068 0.88 1375 128 0.3224 0.3628 REMARK 3 11 3.4068 - 3.3003 0.86 1354 124 0.3523 0.3624 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.970 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 3781 REMARK 3 ANGLE : 0.494 5130 REMARK 3 CHIRALITY : 0.039 597 REMARK 3 PLANARITY : 0.005 634 REMARK 3 DIHEDRAL : 12.561 2228 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 228.6574 16.6097 96.5727 REMARK 3 T TENSOR REMARK 3 T11: 0.6506 T22: 0.3866 REMARK 3 T33: 0.6090 T12: -0.0298 REMARK 3 T13: 0.0376 T23: 0.0691 REMARK 3 L TENSOR REMARK 3 L11: 1.7744 L22: 0.6489 REMARK 3 L33: 3.5909 L12: 1.0331 REMARK 3 L13: 2.1998 L23: 1.3564 REMARK 3 S TENSOR REMARK 3 S11: -0.0182 S12: -0.0725 S13: 0.0265 REMARK 3 S21: 0.1158 S22: -0.0393 S23: 0.0096 REMARK 3 S31: -0.1396 S32: -0.1072 S33: 0.0805 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5T04 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-16. REMARK 100 THE DEPOSITION ID IS D_1000223387. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-JUN-15; 26-FEB-15 REMARK 200 TEMPERATURE (KELVIN) : 90; 90 REMARK 200 PH : 8.5-9.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; APS REMARK 200 BEAMLINE : 23-ID-D; 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332; 1.0332 REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL; CCD REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M; MARMOSAIC REMARK 200 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10042 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 38.141 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 7.100 REMARK 200 R MERGE (I) : 0.18000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.3 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.72000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4XEE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 13-16% (V/V) PEG 400, 80 MM TRISHCL PH REMARK 280 8.5-9.0, 1.9 MM TCEP, 68-91 MM LITHIUM ACETATE, 0.9 MM REMARK 280 NEUROTENSIN, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 52.09500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.85500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.09500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.85500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23190 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A 33 REMARK 465 TYR A 34 REMARK 465 LYS A 35 REMARK 465 ASP A 36 REMARK 465 ASP A 37 REMARK 465 ASP A 38 REMARK 465 ASP A 39 REMARK 465 ALA A 40 REMARK 465 THR A 41 REMARK 465 SER A 42 REMARK 465 LYS A 92 REMARK 465 LYS A 93 REMARK 465 SER A 94 REMARK 465 LEU A 95 REMARK 465 GLN A 96 REMARK 465 SER A 97 REMARK 465 LEU A 98 REMARK 465 GLN A 99 REMARK 465 SER A 373 REMARK 465 ALA A 374 REMARK 465 ASN A 375 REMARK 465 PHE A 376 REMARK 465 ARG A 377 REMARK 465 GLN A 378 REMARK 465 VAL A 379 REMARK 465 PHE A 380 REMARK 465 LEU A 381 REMARK 465 SER A 382 REMARK 465 THR A 383 REMARK 465 LEU A 384 REMARK 465 ALA A 385 REMARK 465 CYS A 386 REMARK 465 LEU A 387 REMARK 465 CYS A 388 REMARK 465 PRO A 389 REMARK 465 GLY A 390 REMARK 465 TRP A 391 REMARK 465 ARG A 392 REMARK 465 HIS A 393 REMARK 465 ARG A 394 REMARK 465 ARG A 395 REMARK 465 LYS A 396 REMARK 465 ALA A 397 REMARK 465 HIS A 398 REMARK 465 HIS A 399 REMARK 465 HIS A 400 REMARK 465 HIS A 401 REMARK 465 HIS A 402 REMARK 465 HIS A 403 REMARK 465 HIS A 404 REMARK 465 HIS A 405 REMARK 465 HIS A 406 REMARK 465 HIS A 407 REMARK 465 GLY A 408 REMARK 465 GLY A 409 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OG1 THR A 48 OG1 THR A 48 2955 1.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 44 -47.83 85.65 REMARK 500 GLU A 45 6.42 58.76 REMARK 500 ILE A1029 31.18 -98.89 REMARK 500 THR A1054 -55.06 61.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TCE A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1204 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4XEE RELATED DB: PDB DBREF 5T04 A 43 268 UNP P20789 NTR1_RAT 43 268 DBREF 5T04 A 1002 1161 UNP P00720 ENLYS_BPT4 2 161 DBREF 5T04 A 297 396 UNP P20789 NTR1_RAT 297 396 DBREF 5T04 B 8 13 PDB 5T04 5T04 8 13 SEQADV 5T04 ASP A 33 UNP P20789 EXPRESSION TAG SEQADV 5T04 TYR A 34 UNP P20789 EXPRESSION TAG SEQADV 5T04 LYS A 35 UNP P20789 EXPRESSION TAG SEQADV 5T04 ASP A 36 UNP P20789 EXPRESSION TAG SEQADV 5T04 ASP A 37 UNP P20789 EXPRESSION TAG SEQADV 5T04 ASP A 38 UNP P20789 EXPRESSION TAG SEQADV 5T04 ASP A 39 UNP P20789 EXPRESSION TAG SEQADV 5T04 ALA A 40 UNP P20789 EXPRESSION TAG SEQADV 5T04 THR A 41 UNP P20789 EXPRESSION TAG SEQADV 5T04 SER A 42 UNP P20789 EXPRESSION TAG SEQADV 5T04 LEU A 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 5T04 ALA A 215 UNP P20789 GLY 215 ENGINEERED MUTATION SEQADV 5T04 GLY A 1012 UNP P00720 ARG 12 ENGINEERED MUTATION SEQADV 5T04 THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 5T04 ALA A 1097 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 5T04 ASN A 1122 UNP P00720 GLN 122 ENGINEERED MUTATION SEQADV 5T04 ASN A 1123 UNP P00720 GLN 123 ENGINEERED MUTATION SEQADV 5T04 ARG A 1137 UNP P00720 ILE 137 ENGINEERED MUTATION SEQADV 5T04 GLY A 1162 UNP P00720 LINKER SEQADV 5T04 SER A 1163 UNP P00720 LINKER SEQADV 5T04 GLY A 1164 UNP P00720 LINKER SEQADV 5T04 SER A 1165 UNP P00720 LINKER SEQADV 5T04 ALA A 358 UNP P20789 PHE 358 ENGINEERED MUTATION SEQADV 5T04 ALA A 360 UNP P20789 VAL 360 ENGINEERED MUTATION SEQADV 5T04 ALA A 397 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 398 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 399 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 400 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 401 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 402 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 403 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 404 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 405 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 406 UNP P20789 EXPRESSION TAG SEQADV 5T04 HIS A 407 UNP P20789 EXPRESSION TAG SEQADV 5T04 GLY A 408 UNP P20789 EXPRESSION TAG SEQADV 5T04 GLY A 409 UNP P20789 EXPRESSION TAG SEQRES 1 A 513 ASP TYR LYS ASP ASP ASP ASP ALA THR SER THR SER GLU SEQRES 2 A 513 SER ASP THR ALA GLY PRO ASN SER ASP LEU ASP VAL ASN SEQRES 3 A 513 THR ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR SEQRES 4 A 513 LEU ALA LEU PHE VAL VAL GLY THR VAL GLY ASN SER VAL SEQRES 5 A 513 THR LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER SEQRES 6 A 513 LEU GLN SER THR VAL HIS TYR HIS LEU GLY SER LEU ALA SEQRES 7 A 513 LEU SER ASP LEU LEU ILE LEU LEU LEU ALA MET PRO VAL SEQRES 8 A 513 GLU LEU TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA SEQRES 9 A 513 PHE GLY ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG SEQRES 10 A 513 ASP ALA CYS THR TYR ALA THR ALA LEU ASN VAL ALA SER SEQRES 11 A 513 LEU SER VAL GLU ARG TYR LEU ALA ILE CYS HIS PRO PHE SEQRES 12 A 513 LYS ALA LYS THR LEU MET SER ARG SER ARG THR LYS LYS SEQRES 13 A 513 PHE ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA SEQRES 14 A 513 ILE PRO MET LEU PHE THR MET GLY LEU GLN ASN ARG SER SEQRES 15 A 513 ALA ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO SEQRES 16 A 513 ILE VAL ASP THR ALA THR VAL LYS VAL VAL ILE GLN VAL SEQRES 17 A 513 ASN THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ILE SEQRES 18 A 513 SER ILE LEU ASN THR VAL ILE ALA ASN LYS LEU THR VAL SEQRES 19 A 513 MET VAL ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY SEQRES 20 A 513 LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR SEQRES 21 A 513 THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER SEQRES 22 A 513 LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY SEQRES 23 A 513 ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU SEQRES 24 A 513 LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY SEQRES 25 A 513 ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER SEQRES 26 A 513 LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL SEQRES 27 A 513 PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SEQRES 28 A 513 SER LEU ARG MET LEU ASN ASN LYS ARG TRP ASP GLU ALA SEQRES 29 A 513 ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR SEQRES 30 A 513 PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR SEQRES 31 A 513 GLY THR TRP ASP ALA TYR GLY SER GLY SER PRO GLY ARG SEQRES 32 A 513 VAL GLN ALA LEU ARG HIS GLY VAL LEU VAL LEU ARG ALA SEQRES 33 A 513 VAL VAL ILE ALA PHE VAL VAL CYS TRP LEU PRO TYR HIS SEQRES 34 A 513 VAL ARG ARG LEU MET PHE CYS TYR ILE SER ASP GLU GLN SEQRES 35 A 513 TRP THR THR PHE LEU PHE ASP PHE TYR HIS TYR PHE TYR SEQRES 36 A 513 MET LEU THR ASN ALA LEU ALA TYR ALA SER SER ALA ILE SEQRES 37 A 513 ASN PRO ILE LEU TYR ASN LEU VAL SER ALA ASN PHE ARG SEQRES 38 A 513 GLN VAL PHE LEU SER THR LEU ALA CYS LEU CYS PRO GLY SEQRES 39 A 513 TRP ARG HIS ARG ARG LYS ALA HIS HIS HIS HIS HIS HIS SEQRES 40 A 513 HIS HIS HIS HIS GLY GLY SEQRES 1 B 6 ARG ARG PRO TYR ILE LEU HET TCE A1201 16 HET GOL A1202 6 HET PEG A1203 7 HET PEG A1204 7 HET PEG A1205 7 HETNAM TCE 3,3',3''-PHOSPHANETRIYLTRIPROPANOIC ACID HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN TCE 3-[BIS(2-CARBOXYETHYL)PHOSPHANYL]PROPANOIC ACID HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 TCE C9 H15 O6 P FORMUL 4 GOL C3 H8 O3 FORMUL 5 PEG 3(C4 H10 O3) HELIX 1 AA1 ASN A 52 ASP A 56 5 5 HELIX 2 AA2 ASP A 60 ALA A 90 1 31 HELIX 3 AA3 THR A 101 PHE A 128 1 28 HELIX 4 AA4 PHE A 137 CYS A 172 1 36 HELIX 5 AA5 SER A 182 ALA A 201 1 20 HELIX 6 AA6 PRO A 203 THR A 207 1 5 HELIX 7 AA7 ASP A 230 PHE A 246 1 17 HELIX 8 AA8 PHE A 246 GLU A 1011 1 33 HELIX 9 AA9 SER A 1038 LEU A 1046 1 9 HELIX 10 AB1 THR A 1059 ARG A 1080 1 22 HELIX 11 AB2 LEU A 1084 LEU A 1091 1 8 HELIX 12 AB3 ASP A 1092 GLY A 1107 1 16 HELIX 13 AB4 GLY A 1107 PHE A 1114 1 8 HELIX 14 AB5 THR A 1115 ASN A 1123 1 9 HELIX 15 AB6 ARG A 1125 ALA A 1134 1 10 HELIX 16 AB7 SER A 1136 THR A 1142 1 7 HELIX 17 AB8 THR A 1142 GLY A 1156 1 15 HELIX 18 AB9 TRP A 1158 GLY A 1162 5 5 HELIX 19 AC1 SER A 1165 ILE A 334 1 39 HELIX 20 AC2 SER A 335 TRP A 339 5 5 HELIX 21 AC3 THR A 340 TYR A 369 1 30 HELIX 22 AC4 ASN A 370 VAL A 372 5 3 SHEET 1 AA1 2 MET A 208 ASN A 212 0 SHEET 2 AA1 2 LEU A 223 PRO A 227 -1 O VAL A 224 N GLN A 211 SHEET 1 AA2 3 ARG A1014 LYS A1019 0 SHEET 2 AA2 3 TYR A1025 GLY A1028 -1 O GLY A1028 N ARG A1014 SHEET 3 AA2 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 142 CYS A 225 1555 1555 2.04 CISPEP 1 HIS A 133 PRO A 134 0 2.19 SITE 1 AC1 7 MET A1106 GLY A1113 PHE A1114 LYS A1135 SITE 2 AC1 7 SER A1136 ARG A1137 TRP A1138 SITE 1 AC2 2 ARG A 143 PHE A 206 SITE 1 AC3 2 PHE A 342 PHE A 346 SITE 1 AC4 2 ASP A 60 TYR A 349 CRYST1 104.190 75.710 83.200 90.00 90.00 90.00 P 21 21 2 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.009598 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013208 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012019 0.00000 ATOM 1 N THR A 43 212.539 8.259 44.593 1.00 94.70 N ANISOU 1 N THR A 43 11175 14034 10772 -3475 524 884 N ATOM 2 CA THR A 43 212.016 7.691 43.356 1.00 97.87 C ANISOU 2 CA THR A 43 11466 14612 11108 -3560 564 841 C ATOM 3 C THR A 43 211.057 6.541 43.673 1.00104.45 C ANISOU 3 C THR A 43 12197 15305 12183 -3192 665 724 C ATOM 4 O THR A 43 211.009 6.066 44.810 1.00103.08 O ANISOU 4 O THR A 43 12002 14965 12199 -2910 721 650 O ATOM 5 CB THR A 43 213.165 7.204 42.437 1.00 98.69 C ANISOU 5 CB THR A 43 11309 15200 10989 -3837 677 670 C ATOM 6 OG1 THR A 43 214.244 8.144 42.488 1.00101.39 O ANISOU 6 OG1 THR A 43 11712 15697 11114 -4157 613 742 O ATOM 7 CG2 THR A 43 212.704 7.081 40.988 1.00 97.01 C ANISOU 7 CG2 THR A 43 11048 15188 10624 -4056 665 694 C ATOM 8 N SER A 44 210.281 6.146 42.656 1.00107.88 N ANISOU 8 N SER A 44 12587 15808 12594 -3225 673 724 N ATOM 9 CA SER A 44 209.335 5.031 42.653 1.00109.79 C ANISOU 9 CA SER A 44 12728 15973 13015 -2954 761 621 C ATOM 10 C SER A 44 207.970 5.429 43.194 1.00110.97 C ANISOU 10 C SER A 44 13069 15772 13321 -2742 666 761 C ATOM 11 O SER A 44 206.948 5.093 42.584 1.00112.20 O ANISOU 11 O SER A 44 13219 15898 13515 -2684 661 775 O ATOM 12 CB SER A 44 209.860 3.823 43.438 1.00115.66 C ANISOU 12 CB SER A 44 13284 16761 13900 -2718 897 402 C ATOM 13 OG SER A 44 211.007 3.274 42.818 1.00117.92 O ANISOU 13 OG SER A 44 13346 17407 14052 -2864 980 211 O ATOM 14 N GLU A 45 207.929 6.111 44.340 1.00106.46 N ANISOU 14 N GLU A 45 12651 14959 12841 -2615 592 841 N ATOM 15 CA GLU A 45 206.688 6.380 45.063 1.00103.66 C ANISOU 15 CA GLU A 45 12430 14311 12646 -2366 518 912 C ATOM 16 C GLU A 45 205.984 5.089 45.435 1.00 97.35 C ANISOU 16 C GLU A 45 11486 13497 12007 -2121 653 781 C ATOM 17 O GLU A 45 204.844 5.106 45.908 1.00 91.04 O ANISOU 17 O GLU A 45 10745 12527 11319 -1931 619 808 O ATOM 18 CB GLU A 45 205.752 7.269 44.243 1.00105.05 C ANISOU 18 CB GLU A 45 12773 14387 12754 -2452 343 1060 C ATOM 19 CG GLU A 45 205.950 8.741 44.475 1.00103.28 C ANISOU 19 CG GLU A 45 12802 13986 12455 -2561 127 1222 C ATOM 20 CD GLU A 45 204.646 9.457 44.657 1.00102.76 C ANISOU 20 CD GLU A 45 12912 13656 12476 -2378 -60 1300 C ATOM 21 OE1 GLU A 45 204.632 10.538 45.275 1.00 98.08 O ANISOU 21 OE1 GLU A 45 12525 12847 11896 -2335 -244 1387 O ATOM 22 OE2 GLU A 45 203.630 8.920 44.183 1.00103.11 O ANISOU 22 OE2 GLU A 45 12882 13719 12576 -2265 -29 1258 O ATOM 23 N SER A 46 206.644 3.974 45.178 1.00102.28 N ANISOU 23 N SER A 46 11921 14314 12626 -2138 789 628 N ATOM 24 CA SER A 46 206.183 2.647 45.527 1.00102.52 C ANISOU 24 CA SER A 46 11833 14329 12792 -1940 895 498 C ATOM 25 C SER A 46 207.209 1.960 46.413 1.00 99.80 C ANISOU 25 C SER A 46 11405 14006 12511 -1851 965 364 C ATOM 26 O SER A 46 206.938 0.856 46.907 1.00 89.57 O ANISOU 26 O SER A 46 10048 12652 11331 -1686 1021 262 O ATOM 27 CB SER A 46 205.926 1.856 44.223 1.00105.26 C ANISOU 27 CB SER A 46 12046 14870 13078 -2028 948 418 C ATOM 28 OG SER A 46 207.121 1.670 43.480 1.00107.40 O ANISOU 28 OG SER A 46 12182 15408 13216 -2208 990 312 O ATOM 29 N ASP A 47 208.356 2.598 46.647 1.00 98.41 N ANISOU 29 N ASP A 47 11237 13899 12254 -1962 946 368 N ATOM 30 CA ASP A 47 209.373 2.074 47.540 1.00 98.27 C ANISOU 30 CA ASP A 47 11148 13897 12293 -1869 992 241 C ATOM 31 C ASP A 47 209.305 2.904 48.807 1.00 95.55 C ANISOU 31 C ASP A 47 10963 13324 12017 -1782 939 359 C ATOM 32 O ASP A 47 209.383 4.133 48.742 1.00 93.64 O ANISOU 32 O ASP A 47 10846 13041 11691 -1908 857 496 O ATOM 33 CB ASP A 47 210.765 2.147 46.893 1.00 96.43 C ANISOU 33 CB ASP A 47 10774 13961 11904 -2060 1017 126 C ATOM 34 CG ASP A 47 211.887 1.789 47.844 1.00 89.79 C ANISOU 34 CG ASP A 47 9864 13143 11111 -1963 1042 -8 C ATOM 35 OD1 ASP A 47 211.629 1.532 49.037 1.00 84.29 O ANISOU 35 OD1 ASP A 47 9251 12209 10566 -1762 1033 10 O ATOM 36 OD2 ASP A 47 213.055 1.724 47.393 1.00 90.22 O ANISOU 36 OD2 ASP A 47 9764 13475 11039 -2091 1068 -149 O ATOM 37 N THR A 48 209.118 2.242 49.947 1.00 94.05 N ANISOU 37 N THR A 48 10784 12979 11971 -1578 967 308 N ATOM 38 CA THR A 48 209.069 3.016 51.175 1.00 94.26 C ANISOU 38 CA THR A 48 10947 12814 12055 -1497 922 404 C ATOM 39 C THR A 48 210.467 3.203 51.743 1.00 93.91 C ANISOU 39 C THR A 48 10873 12828 11980 -1536 928 345 C ATOM 40 O THR A 48 210.829 4.304 52.161 1.00 98.89 O ANISOU 40 O THR A 48 11611 13398 12564 -1604 871 445 O ATOM 41 CB THR A 48 208.174 2.331 52.199 1.00 93.74 C ANISOU 41 CB THR A 48 10914 12574 12130 -1297 944 393 C ATOM 42 OG1 THR A 48 208.413 0.927 52.164 1.00 94.68 O ANISOU 42 OG1 THR A 48 10928 12743 12303 -1232 996 252 O ATOM 43 CG2 THR A 48 206.715 2.563 51.851 1.00 92.68 C ANISOU 43 CG2 THR A 48 10829 12377 12008 -1263 919 473 C ATOM 44 N ALA A 49 211.258 2.134 51.764 1.00 87.49 N ANISOU 44 N ALA A 49 9920 12130 11192 -1486 981 172 N ATOM 45 CA ALA A 49 212.644 2.188 52.225 1.00 84.67 C ANISOU 45 CA ALA A 49 9499 11873 10800 -1510 985 74 C ATOM 46 C ALA A 49 213.514 2.499 51.015 1.00 83.26 C ANISOU 46 C ALA A 49 9188 12006 10440 -1736 1000 5 C ATOM 47 O ALA A 49 214.023 1.603 50.338 1.00 89.75 O ANISOU 47 O ALA A 49 9829 13042 11228 -1736 1037 -187 O ATOM 48 CB ALA A 49 213.042 0.879 52.891 1.00 81.43 C ANISOU 48 CB ALA A 49 9011 11422 10508 -1320 997 -101 C ATOM 49 N GLY A 50 213.679 3.788 50.733 1.00 76.05 N ANISOU 49 N GLY A 50 8372 11127 9395 -1942 956 156 N ATOM 50 CA GLY A 50 214.370 4.222 49.543 1.00 69.28 C ANISOU 50 CA GLY A 50 7420 10577 8326 -2225 958 132 C ATOM 51 C GLY A 50 215.872 4.294 49.715 1.00 66.29 C ANISOU 51 C GLY A 50 6904 10450 7835 -2334 985 -7 C ATOM 52 O GLY A 50 216.491 3.465 50.391 1.00 65.62 O ANISOU 52 O GLY A 50 6702 10385 7845 -2149 1021 -188 O ATOM 53 N PRO A 51 216.501 5.315 49.081 1.00 65.39 N ANISOU 53 N PRO A 51 6808 10542 7496 -2658 951 75 N ATOM 54 CA PRO A 51 217.963 5.485 49.147 1.00 65.47 C ANISOU 54 CA PRO A 51 6666 10858 7350 -2819 980 -61 C ATOM 55 C PRO A 51 218.421 6.129 50.453 1.00 69.92 C ANISOU 55 C PRO A 51 7366 11222 7977 -2752 939 23 C ATOM 56 O PRO A 51 218.995 7.221 50.478 1.00 71.04 O ANISOU 56 O PRO A 51 7604 11431 7958 -3007 884 144 O ATOM 57 CB PRO A 51 218.239 6.368 47.925 1.00 65.40 C ANISOU 57 CB PRO A 51 6663 11128 7056 -3239 945 38 C ATOM 58 CG PRO A 51 217.015 7.200 47.800 1.00 65.37 C ANISOU 58 CG PRO A 51 6948 10794 7095 -3274 835 319 C ATOM 59 CD PRO A 51 215.867 6.315 48.205 1.00 65.43 C ANISOU 59 CD PRO A 51 6975 10523 7364 -2911 868 291 C ATOM 60 N ASN A 52 218.161 5.441 51.564 1.00 72.64 N ANISOU 60 N ASN A 52 7730 11318 8551 -2422 957 -37 N ATOM 61 CA ASN A 52 218.557 5.896 52.891 1.00 74.33 C ANISOU 61 CA ASN A 52 8058 11337 8847 -2321 927 20 C ATOM 62 C ASN A 52 219.658 5.019 53.479 1.00 70.88 C ANISOU 62 C ASN A 52 7424 11052 8456 -2173 975 -230 C ATOM 63 O ASN A 52 219.771 4.886 54.700 1.00 66.28 O ANISOU 63 O ASN A 52 6914 10254 8015 -1977 959 -228 O ATOM 64 CB ASN A 52 217.348 5.928 53.826 1.00 76.70 C ANISOU 64 CB ASN A 52 8561 11223 9357 -2080 890 167 C ATOM 65 CG ASN A 52 216.197 6.749 53.271 1.00 76.27 C ANISOU 65 CG ASN A 52 8691 11014 9275 -2174 819 377 C ATOM 66 OD1 ASN A 52 216.405 7.767 52.610 1.00 76.73 O ANISOU 66 OD1 ASN A 52 8835 11157 9162 -2440 749 499 O ATOM 67 ND2 ASN A 52 214.973 6.307 53.537 1.00 72.97 N ANISOU 67 ND2 ASN A 52 8338 10373 9015 -1965 819 417 N ATOM 68 N SER A 53 220.480 4.417 52.616 1.00 76.56 N ANISOU 68 N SER A 53 7886 12154 9049 -2260 1021 -464 N ATOM 69 CA SER A 53 221.458 3.439 53.080 1.00 86.75 C ANISOU 69 CA SER A 53 8970 13593 10398 -2067 1036 -753 C ATOM 70 C SER A 53 222.547 4.073 53.938 1.00 90.25 C ANISOU 70 C SER A 53 9409 14102 10779 -2127 1024 -767 C ATOM 71 O SER A 53 223.060 3.425 54.857 1.00 93.49 O ANISOU 71 O SER A 53 9767 14435 11319 -1888 1003 -917 O ATOM 72 CB SER A 53 222.079 2.718 51.884 1.00 93.37 C ANISOU 72 CB SER A 53 9510 14870 11097 -2143 1075 -1035 C ATOM 73 OG SER A 53 222.745 3.634 51.034 1.00 98.07 O ANISOU 73 OG SER A 53 10012 15841 11409 -2522 1107 -1011 O ATOM 74 N ASP A 54 222.910 5.329 53.663 1.00 92.72 N ANISOU 74 N ASP A 54 9793 14545 10891 -2452 1020 -607 N ATOM 75 CA ASP A 54 223.982 5.972 54.416 1.00 95.18 C ANISOU 75 CA ASP A 54 10097 14948 11119 -2545 1009 -619 C ATOM 76 C ASP A 54 223.583 6.293 55.851 1.00 89.61 C ANISOU 76 C ASP A 54 9630 13805 10612 -2340 963 -452 C ATOM 77 O ASP A 54 224.461 6.569 56.676 1.00 93.91 O ANISOU 77 O ASP A 54 10158 14382 11142 -2331 955 -497 O ATOM 78 CB ASP A 54 224.434 7.251 53.709 1.00104.82 C ANISOU 78 CB ASP A 54 11364 16413 12051 -2991 994 -471 C ATOM 79 CG ASP A 54 225.187 6.971 52.425 1.00116.14 C ANISOU 79 CG ASP A 54 12504 18394 13229 -3246 1052 -685 C ATOM 80 OD1 ASP A 54 225.543 5.797 52.188 1.00121.56 O ANISOU 80 OD1 ASP A 54 12923 19293 13972 -3042 1100 -993 O ATOM 81 OD2 ASP A 54 225.428 7.924 51.654 1.00119.66 O ANISOU 81 OD2 ASP A 54 12992 19063 13409 -3659 1032 -554 O ATOM 82 N LEU A 55 222.291 6.266 56.168 1.00 80.69 N ANISOU 82 N LEU A 55 8706 12297 9654 -2182 936 -275 N ATOM 83 CA LEU A 55 221.821 6.555 57.515 1.00 72.87 C ANISOU 83 CA LEU A 55 7925 10925 8839 -1993 896 -132 C ATOM 84 C LEU A 55 221.643 5.303 58.365 1.00 70.62 C ANISOU 84 C LEU A 55 7594 10470 8769 -1657 904 -271 C ATOM 85 O LEU A 55 221.351 5.422 59.559 1.00 68.83 O ANISOU 85 O LEU A 55 7515 9964 8675 -1506 877 -180 O ATOM 86 CB LEU A 55 220.492 7.322 57.459 1.00 71.47 C ANISOU 86 CB LEU A 55 7992 10455 8707 -2019 846 125 C ATOM 87 CG LEU A 55 220.476 8.664 56.723 1.00 69.57 C ANISOU 87 CG LEU A 55 7884 10275 8273 -2340 777 311 C ATOM 88 CD1 LEU A 55 219.056 9.200 56.616 1.00 66.99 C ANISOU 88 CD1 LEU A 55 7778 9650 8024 -2289 701 510 C ATOM 89 CD2 LEU A 55 221.382 9.671 57.413 1.00 69.89 C ANISOU 89 CD2 LEU A 55 8018 10318 8219 -2487 727 384 C ATOM 90 N ASP A 56 221.813 4.117 57.785 1.00 73.59 N ANISOU 90 N ASP A 56 7782 11005 9173 -1548 922 -492 N ATOM 91 CA ASP A 56 221.550 2.879 58.504 1.00 77.50 C ANISOU 91 CA ASP A 56 8278 11302 9866 -1249 887 -608 C ATOM 92 C ASP A 56 222.620 2.617 59.557 1.00 80.39 C ANISOU 92 C ASP A 56 8597 11666 10280 -1118 846 -744 C ATOM 93 O ASP A 56 223.785 2.992 59.402 1.00 85.70 O ANISOU 93 O ASP A 56 9124 12617 10821 -1231 859 -867 O ATOM 94 CB ASP A 56 221.477 1.704 57.529 1.00 79.31 C ANISOU 94 CB ASP A 56 8335 11694 10106 -1168 883 -821 C ATOM 95 CG ASP A 56 220.301 1.807 56.574 1.00 81.90 C ANISOU 95 CG ASP A 56 8720 11986 10412 -1263 919 -686 C ATOM 96 OD1 ASP A 56 219.303 2.469 56.929 1.00 85.41 O ANISOU 96 OD1 ASP A 56 9365 12185 10902 -1293 923 -443 O ATOM 97 OD2 ASP A 56 220.373 1.228 55.468 1.00 81.18 O ANISOU 97 OD2 ASP A 56 8465 12124 10256 -1300 936 -840 O ATOM 98 N VAL A 57 222.207 1.963 60.641 1.00 75.98 N ANISOU 98 N VAL A 57 8166 10803 9901 -895 791 -721 N ATOM 99 CA VAL A 57 223.085 1.601 61.748 1.00 73.80 C ANISOU 99 CA VAL A 57 7882 10462 9696 -742 726 -835 C ATOM 100 C VAL A 57 223.033 0.090 61.922 1.00 80.15 C ANISOU 100 C VAL A 57 8658 11154 10640 -496 621 -1024 C ATOM 101 O VAL A 57 221.951 -0.507 61.901 1.00 84.78 O ANISOU 101 O VAL A 57 9362 11529 11320 -428 599 -938 O ATOM 102 CB VAL A 57 222.681 2.325 63.049 1.00 72.60 C ANISOU 102 CB VAL A 57 7950 10022 9614 -730 726 -608 C ATOM 103 CG1 VAL A 57 223.503 1.824 64.218 1.00 73.93 C ANISOU 103 CG1 VAL A 57 8126 10097 9868 -563 647 -719 C ATOM 104 CG2 VAL A 57 222.826 3.831 62.884 1.00 71.62 C ANISOU 104 CG2 VAL A 57 7873 9987 9353 -961 786 -440 C ATOM 105 N ASN A 58 224.202 -0.528 62.098 1.00 81.04 N ANISOU 105 N ASN A 58 8622 11410 10759 -365 538 -1289 N ATOM 106 CA ASN A 58 224.338 -1.980 62.069 1.00 83.19 C ANISOU 106 CA ASN A 58 8851 11610 11146 -125 391 -1524 C ATOM 107 C ASN A 58 224.271 -2.618 63.455 1.00 84.54 C ANISOU 107 C ASN A 58 9221 11426 11474 64 251 -1486 C ATOM 108 O ASN A 58 224.781 -3.730 63.633 1.00 87.44 O ANISOU 108 O ASN A 58 9558 11737 11926 277 78 -1718 O ATOM 109 CB ASN A 58 225.651 -2.371 61.387 1.00 84.27 C ANISOU 109 CB ASN A 58 8693 12128 11197 -58 343 -1889 C ATOM 110 CG ASN A 58 225.691 -1.969 59.927 1.00 86.18 C ANISOU 110 CG ASN A 58 8725 12751 11267 -256 462 -1960 C ATOM 111 OD1 ASN A 58 224.791 -2.289 59.150 1.00 85.49 O ANISOU 111 OD1 ASN A 58 8667 12623 11193 -289 489 -1902 O ATOM 112 ND2 ASN A 58 226.744 -1.254 59.548 1.00 88.18 N ANISOU 112 ND2 ASN A 58 8767 13396 11343 -412 533 -2082 N ATOM 113 N THR A 59 223.671 -1.945 64.436 1.00 82.61 N ANISOU 113 N THR A 59 9180 10945 11261 -10 303 -1211 N ATOM 114 CA THR A 59 223.556 -2.521 65.771 1.00 81.98 C ANISOU 114 CA THR A 59 9297 10545 11306 126 175 -1155 C ATOM 115 C THR A 59 222.680 -3.767 65.746 1.00 84.90 C ANISOU 115 C THR A 59 9804 10676 11779 228 48 -1156 C ATOM 116 O THR A 59 221.640 -3.803 65.084 1.00 89.96 O ANISOU 116 O THR A 59 10475 11300 12404 140 121 -1046 O ATOM 117 CB THR A 59 222.979 -1.499 66.753 1.00 79.03 C ANISOU 117 CB THR A 59 9093 10008 10925 6 272 -868 C ATOM 118 OG1 THR A 59 221.780 -0.929 66.210 1.00 76.86 O ANISOU 118 OG1 THR A 59 8873 9720 10611 -136 396 -671 O ATOM 119 CG2 THR A 59 223.994 -0.398 67.047 1.00 83.90 C ANISOU 119 CG2 THR A 59 9622 10800 11457 -71 343 -876 C ATOM 120 N ASP A 60 223.104 -4.790 66.482 1.00 81.91 N ANISOU 120 N ASP A 60 9522 10102 11497 404 -161 -1279 N ATOM 121 CA ASP A 60 222.388 -6.057 66.490 1.00 84.43 C ANISOU 121 CA ASP A 60 10001 10176 11904 488 -331 -1291 C ATOM 122 C ASP A 60 221.078 -5.943 67.262 1.00 82.90 C ANISOU 122 C ASP A 60 10047 9730 11721 347 -283 -982 C ATOM 123 O ASP A 60 220.941 -5.140 68.189 1.00 84.34 O ANISOU 123 O ASP A 60 10310 9854 11880 258 -195 -802 O ATOM 124 CB ASP A 60 223.255 -7.153 67.106 1.00 91.45 C ANISOU 124 CB ASP A 60 10960 10899 12887 711 -615 -1508 C ATOM 125 CG ASP A 60 224.474 -7.468 66.267 1.00 98.71 C ANISOU 125 CG ASP A 60 11615 12094 13797 886 -695 -1878 C ATOM 126 OD1 ASP A 60 224.332 -8.202 65.266 1.00100.37 O ANISOU 126 OD1 ASP A 60 11738 12378 14019 965 -766 -2054 O ATOM 127 OD2 ASP A 60 225.573 -6.979 66.605 1.00103.44 O ANISOU 127 OD2 ASP A 60 12079 12857 14365 943 -686 -2006 O ATOM 128 N ILE A 61 220.105 -6.770 66.871 1.00 79.69 N ANISOU 128 N ILE A 61 9745 9194 11339 322 -345 -937 N ATOM 129 CA ILE A 61 218.840 -6.810 67.592 1.00 76.21 C ANISOU 129 CA ILE A 61 9516 8554 10887 175 -316 -675 C ATOM 130 C ILE A 61 219.012 -7.436 68.969 1.00 75.26 C ANISOU 130 C ILE A 61 9625 8158 10811 202 -511 -620 C ATOM 131 O ILE A 61 218.232 -7.141 69.880 1.00 75.90 O ANISOU 131 O ILE A 61 9851 8134 10853 57 -456 -402 O ATOM 132 CB ILE A 61 217.771 -7.556 66.766 1.00 76.08 C ANISOU 132 CB ILE A 61 9542 8497 10866 119 -335 -648 C ATOM 133 CG1 ILE A 61 216.369 -7.277 67.318 1.00 74.84 C ANISOU 133 CG1 ILE A 61 9526 8255 10655 -74 -231 -382 C ATOM 134 CG2 ILE A 61 218.054 -9.051 66.733 1.00 76.33 C ANISOU 134 CG2 ILE A 61 9701 8328 10975 250 -624 -810 C ATOM 135 CD1 ILE A 61 215.253 -7.837 66.463 1.00 75.10 C ANISOU 135 CD1 ILE A 61 9576 8295 10664 -155 -213 -342 C ATOM 136 N TYR A 62 220.026 -8.286 69.151 1.00 75.71 N ANISOU 136 N TYR A 62 9715 8110 10941 383 -751 -826 N ATOM 137 CA TYR A 62 220.287 -8.854 70.469 1.00 78.17 C ANISOU 137 CA TYR A 62 10262 8147 11291 407 -966 -774 C ATOM 138 C TYR A 62 220.676 -7.769 71.464 1.00 82.75 C ANISOU 138 C TYR A 62 10823 8781 11838 350 -831 -657 C ATOM 139 O TYR A 62 220.210 -7.768 72.610 1.00 84.95 O ANISOU 139 O TYR A 62 11297 8888 12091 231 -864 -468 O ATOM 140 CB TYR A 62 221.382 -9.915 70.377 1.00 78.67 C ANISOU 140 CB TYR A 62 10349 8094 11447 653 -1278 -1057 C ATOM 141 CG TYR A 62 221.017 -11.101 69.515 1.00 81.02 C ANISOU 141 CG TYR A 62 10707 8289 11789 728 -1468 -1187 C ATOM 142 CD1 TYR A 62 220.389 -12.212 70.059 1.00 81.86 C ANISOU 142 CD1 TYR A 62 11131 8055 11917 669 -1731 -1088 C ATOM 143 CD2 TYR A 62 221.300 -11.109 68.155 1.00 82.80 C ANISOU 143 CD2 TYR A 62 10680 8761 12018 837 -1397 -1408 C ATOM 144 CE1 TYR A 62 220.053 -13.299 69.274 1.00 83.58 C ANISOU 144 CE1 TYR A 62 11424 8157 12174 734 -1926 -1205 C ATOM 145 CE2 TYR A 62 220.967 -12.190 67.362 1.00 84.33 C ANISOU 145 CE2 TYR A 62 10927 8861 12254 916 -1576 -1540 C ATOM 146 CZ TYR A 62 220.344 -13.283 67.927 1.00 84.50 C ANISOU 146 CZ TYR A 62 11277 8519 12311 872 -1846 -1438 C ATOM 147 OH TYR A 62 220.011 -14.363 67.143 1.00 84.88 O ANISOU 147 OH TYR A 62 11399 8454 12400 946 -2045 -1568 O ATOM 148 N SER A 63 221.531 -6.834 71.045 1.00 85.37 N ANISOU 148 N SER A 63 10921 9362 12152 415 -682 -767 N ATOM 149 CA SER A 63 221.865 -5.709 71.910 1.00 88.28 C ANISOU 149 CA SER A 63 11270 9791 12483 349 -543 -650 C ATOM 150 C SER A 63 220.657 -4.805 72.121 1.00 86.75 C ANISOU 150 C SER A 63 11115 9628 12217 148 -324 -391 C ATOM 151 O SER A 63 220.458 -4.270 73.218 1.00 90.42 O ANISOU 151 O SER A 63 11680 10019 12656 67 -279 -239 O ATOM 152 CB SER A 63 223.035 -4.922 71.323 1.00 92.52 C ANISOU 152 CB SER A 63 11553 10606 12995 428 -444 -826 C ATOM 153 OG SER A 63 222.687 -4.345 70.077 1.00 94.95 O ANISOU 153 OG SER A 63 11684 11152 13241 349 -262 -834 O ATOM 154 N LYS A 64 219.837 -4.625 71.081 1.00 81.17 N ANISOU 154 N LYS A 64 10323 9041 11475 76 -196 -356 N ATOM 155 CA LYS A 64 218.617 -3.838 71.232 1.00 75.68 C ANISOU 155 CA LYS A 64 9660 8379 10716 -86 -19 -144 C ATOM 156 C LYS A 64 217.701 -4.446 72.284 1.00 75.96 C ANISOU 156 C LYS A 64 9907 8218 10735 -189 -99 8 C ATOM 157 O LYS A 64 217.117 -3.724 73.101 1.00 75.61 O ANISOU 157 O LYS A 64 9908 8184 10637 -294 4 157 O ATOM 158 CB LYS A 64 217.891 -3.727 69.892 1.00 72.10 C ANISOU 158 CB LYS A 64 9091 8069 10233 -130 91 -151 C ATOM 159 CG LYS A 64 218.638 -2.930 68.839 1.00 73.44 C ANISOU 159 CG LYS A 64 9054 8474 10377 -100 197 -260 C ATOM 160 CD LYS A 64 217.851 -2.861 67.543 1.00 74.02 C ANISOU 160 CD LYS A 64 9036 8676 10414 -162 291 -251 C ATOM 161 CE LYS A 64 218.624 -2.120 66.468 1.00 75.86 C ANISOU 161 CE LYS A 64 9073 9160 10591 -174 379 -356 C ATOM 162 NZ LYS A 64 217.843 -2.019 65.206 1.00 75.69 N ANISOU 162 NZ LYS A 64 8973 9260 10525 -250 464 -335 N ATOM 163 N VAL A 65 217.563 -5.774 72.279 1.00 76.30 N ANISOU 163 N VAL A 65 10087 8093 10811 -173 -297 -37 N ATOM 164 CA VAL A 65 216.769 -6.447 73.302 1.00 72.43 C ANISOU 164 CA VAL A 65 9824 7419 10276 -318 -406 113 C ATOM 165 C VAL A 65 217.392 -6.241 74.676 1.00 73.05 C ANISOU 165 C VAL A 65 10014 7390 10353 -323 -479 163 C ATOM 166 O VAL A 65 216.691 -5.967 75.659 1.00 72.92 O ANISOU 166 O VAL A 65 10093 7357 10255 -485 -427 325 O ATOM 167 CB VAL A 65 216.619 -7.943 72.966 1.00 70.18 C ANISOU 167 CB VAL A 65 9696 6944 10024 -306 -652 51 C ATOM 168 CG1 VAL A 65 215.958 -8.683 74.115 1.00 70.65 C ANISOU 168 CG1 VAL A 65 10026 6802 10015 -495 -806 213 C ATOM 169 CG2 VAL A 65 215.809 -8.119 71.697 1.00 70.54 C ANISOU 169 CG2 VAL A 65 9642 7104 10056 -336 -560 30 C ATOM 170 N LEU A 66 218.719 -6.356 74.763 1.00 74.16 N ANISOU 170 N LEU A 66 10124 7482 10570 -147 -599 11 N ATOM 171 CA LEU A 66 219.400 -6.196 76.043 1.00 71.11 C ANISOU 171 CA LEU A 66 9843 6987 10188 -137 -685 46 C ATOM 172 C LEU A 66 219.251 -4.775 76.572 1.00 71.24 C ANISOU 172 C LEU A 66 9757 7164 10148 -211 -444 158 C ATOM 173 O LEU A 66 218.936 -4.568 77.750 1.00 72.66 O ANISOU 173 O LEU A 66 10054 7280 10272 -328 -441 292 O ATOM 174 CB LEU A 66 220.875 -6.564 75.897 1.00 69.54 C ANISOU 174 CB LEU A 66 9594 6745 10083 92 -859 -177 C ATOM 175 CG LEU A 66 221.741 -6.298 77.126 1.00 68.70 C ANISOU 175 CG LEU A 66 9563 6552 9989 131 -940 -167 C ATOM 176 CD1 LEU A 66 221.278 -7.154 78.291 1.00 67.70 C ANISOU 176 CD1 LEU A 66 9736 6154 9831 3 -1150 -22 C ATOM 177 CD2 LEU A 66 223.205 -6.550 76.811 1.00 70.15 C ANISOU 177 CD2 LEU A 66 9634 6762 10257 376 -1086 -428 C ATOM 178 N VAL A 67 219.476 -3.779 75.713 1.00 70.03 N ANISOU 178 N VAL A 67 9391 7219 9998 -155 -256 100 N ATOM 179 CA VAL A 67 219.368 -2.390 76.150 1.00 67.95 C ANISOU 179 CA VAL A 67 9050 7083 9686 -211 -63 195 C ATOM 180 C VAL A 67 217.942 -2.076 76.578 1.00 68.64 C ANISOU 180 C VAL A 67 9194 7192 9693 -372 46 361 C ATOM 181 O VAL A 67 217.716 -1.421 77.603 1.00 69.40 O ANISOU 181 O VAL A 67 9330 7298 9742 -440 107 454 O ATOM 182 CB VAL A 67 219.853 -1.443 75.037 1.00 68.35 C ANISOU 182 CB VAL A 67 8896 7336 9739 -151 78 110 C ATOM 183 CG1 VAL A 67 219.509 0.000 75.374 1.00 68.06 C ANISOU 183 CG1 VAL A 67 8815 7397 9647 -223 249 224 C ATOM 184 CG2 VAL A 67 221.345 -1.605 74.839 1.00 68.62 C ANISOU 184 CG2 VAL A 67 8842 7410 9819 -15 -13 -70 C ATOM 185 N THR A 68 216.958 -2.554 75.813 1.00 67.28 N ANISOU 185 N THR A 68 9015 7052 9498 -434 69 383 N ATOM 186 CA THR A 68 215.564 -2.328 76.178 1.00 64.34 C ANISOU 186 CA THR A 68 8669 6743 9034 -588 166 510 C ATOM 187 C THR A 68 215.233 -2.979 77.515 1.00 64.58 C ANISOU 187 C THR A 68 8879 6661 8998 -728 59 605 C ATOM 188 O THR A 68 214.532 -2.387 78.345 1.00 65.93 O ANISOU 188 O THR A 68 9048 6924 9080 -839 153 689 O ATOM 189 CB THR A 68 214.642 -2.853 75.079 1.00 63.38 C ANISOU 189 CB THR A 68 8508 6676 8896 -631 190 503 C ATOM 190 OG1 THR A 68 215.090 -2.365 73.808 1.00 63.42 O ANISOU 190 OG1 THR A 68 8360 6780 8957 -515 263 409 O ATOM 191 CG2 THR A 68 213.217 -2.380 75.315 1.00 64.73 C ANISOU 191 CG2 THR A 68 8647 6982 8966 -767 320 599 C ATOM 192 N ALA A 69 215.735 -4.195 77.747 1.00 64.40 N ANISOU 192 N ALA A 69 9018 6444 9007 -730 -157 583 N ATOM 193 CA ALA A 69 215.525 -4.839 79.040 1.00 63.69 C ANISOU 193 CA ALA A 69 9133 6226 8840 -892 -295 688 C ATOM 194 C ALA A 69 216.226 -4.073 80.153 1.00 63.14 C ANISOU 194 C ALA A 69 9067 6156 8768 -863 -266 710 C ATOM 195 O ALA A 69 215.652 -3.866 81.228 1.00 64.44 O ANISOU 195 O ALA A 69 9295 6366 8822 -1032 -231 817 O ATOM 196 CB ALA A 69 216.013 -6.286 78.998 1.00 64.51 C ANISOU 196 CB ALA A 69 9441 6078 8991 -878 -585 652 C ATOM 197 N ILE A 70 217.467 -3.642 79.912 1.00 62.13 N ANISOU 197 N ILE A 70 8859 6002 8746 -664 -276 599 N ATOM 198 CA ILE A 70 218.169 -2.826 80.898 1.00 61.63 C ANISOU 198 CA ILE A 70 8784 5950 8682 -631 -236 614 C ATOM 199 C ILE A 70 217.440 -1.505 81.104 1.00 62.13 C ANISOU 199 C ILE A 70 8717 6212 8677 -688 -4 675 C ATOM 200 O ILE A 70 217.332 -1.006 82.231 1.00 66.58 O ANISOU 200 O ILE A 70 9317 6802 9178 -764 33 741 O ATOM 201 CB ILE A 70 219.633 -2.611 80.472 1.00 61.37 C ANISOU 201 CB ILE A 70 8665 5892 8760 -417 -287 466 C ATOM 202 CG1 ILE A 70 220.401 -3.933 80.528 1.00 62.25 C ANISOU 202 CG1 ILE A 70 8920 5794 8939 -331 -564 376 C ATOM 203 CG2 ILE A 70 220.305 -1.580 81.361 1.00 60.67 C ANISOU 203 CG2 ILE A 70 8538 5849 8664 -390 -210 484 C ATOM 204 CD1 ILE A 70 221.820 -3.839 80.012 1.00 63.33 C ANISOU 204 CD1 ILE A 70 8934 5956 9173 -108 -626 180 C ATOM 205 N TYR A 71 216.911 -0.928 80.023 1.00 61.23 N ANISOU 205 N TYR A 71 8455 6237 8572 -646 137 644 N ATOM 206 CA TYR A 71 216.159 0.315 80.150 1.00 60.49 C ANISOU 206 CA TYR A 71 8250 6311 8421 -673 315 681 C ATOM 207 C TYR A 71 214.862 0.101 80.916 1.00 61.11 C ANISOU 207 C TYR A 71 8372 6472 8374 -851 348 762 C ATOM 208 O TYR A 71 214.450 0.965 81.698 1.00 61.25 O ANISOU 208 O TYR A 71 8342 6602 8326 -885 438 780 O ATOM 209 CB TYR A 71 215.867 0.903 78.772 1.00 63.06 C ANISOU 209 CB TYR A 71 8435 6745 8780 -595 419 631 C ATOM 210 CG TYR A 71 216.998 1.717 78.191 1.00 68.33 C ANISOU 210 CG TYR A 71 9017 7428 9516 -468 447 564 C ATOM 211 CD1 TYR A 71 218.295 1.582 78.664 1.00 68.55 C ANISOU 211 CD1 TYR A 71 9081 7373 9590 -403 364 518 C ATOM 212 CD2 TYR A 71 216.765 2.629 77.171 1.00 71.34 C ANISOU 212 CD2 TYR A 71 9288 7918 9899 -431 544 546 C ATOM 213 CE1 TYR A 71 219.330 2.326 78.130 1.00 69.20 C ANISOU 213 CE1 TYR A 71 9071 7514 9706 -322 395 450 C ATOM 214 CE2 TYR A 71 217.791 3.377 76.632 1.00 71.19 C ANISOU 214 CE2 TYR A 71 9205 7935 9909 -368 560 498 C ATOM 215 CZ TYR A 71 219.071 3.223 77.114 1.00 69.43 C ANISOU 215 CZ TYR A 71 8999 7661 9718 -322 495 448 C ATOM 216 OH TYR A 71 220.093 3.972 76.576 1.00 70.25 O ANISOU 216 OH TYR A 71 9025 7844 9824 -293 517 394 O ATOM 217 N LEU A 72 214.197 -1.037 80.702 1.00 61.76 N ANISOU 217 N LEU A 72 8536 6521 8408 -976 270 798 N ATOM 218 CA LEU A 72 212.967 -1.310 81.438 1.00 65.01 C ANISOU 218 CA LEU A 72 8980 7055 8666 -1193 299 871 C ATOM 219 C LEU A 72 213.240 -1.446 82.929 1.00 69.05 C ANISOU 219 C LEU A 72 9613 7526 9096 -1321 229 936 C ATOM 220 O LEU A 72 212.457 -0.963 83.757 1.00 71.77 O ANISOU 220 O LEU A 72 9904 8055 9310 -1449 320 958 O ATOM 221 CB LEU A 72 212.289 -2.572 80.900 1.00 68.68 C ANISOU 221 CB LEU A 72 9537 7476 9084 -1333 205 909 C ATOM 222 CG LEU A 72 211.523 -2.443 79.581 1.00 69.93 C ANISOU 222 CG LEU A 72 9559 7750 9262 -1282 306 862 C ATOM 223 CD1 LEU A 72 211.018 -3.801 79.119 1.00 70.64 C ANISOU 223 CD1 LEU A 72 9770 7759 9311 -1424 182 902 C ATOM 224 CD2 LEU A 72 210.374 -1.458 79.722 1.00 68.40 C ANISOU 224 CD2 LEU A 72 9197 7824 8968 -1322 483 845 C ATOM 225 N ALA A 73 214.350 -2.093 83.291 1.00 70.71 N ANISOU 225 N ALA A 73 9979 7511 9376 -1283 58 950 N ATOM 226 CA ALA A 73 214.688 -2.238 84.702 1.00 68.70 C ANISOU 226 CA ALA A 73 9858 7198 9047 -1406 -29 1019 C ATOM 227 C ALA A 73 214.988 -0.886 85.338 1.00 65.00 C ANISOU 227 C ALA A 73 9263 6852 8584 -1312 117 985 C ATOM 228 O ALA A 73 214.507 -0.590 86.438 1.00 62.78 O ANISOU 228 O ALA A 73 8987 6694 8172 -1462 161 1029 O ATOM 229 CB ALA A 73 215.876 -3.186 84.863 1.00 70.47 C ANISOU 229 CB ALA A 73 10275 7137 9365 -1341 -270 1018 C ATOM 230 N LEU A 74 215.770 -0.049 84.655 1.00 62.33 N ANISOU 230 N LEU A 74 8809 6494 8378 -1082 185 902 N ATOM 231 CA LEU A 74 216.090 1.267 85.194 1.00 60.85 C ANISOU 231 CA LEU A 74 8524 6398 8200 -993 300 871 C ATOM 232 C LEU A 74 214.848 2.145 85.285 1.00 62.58 C ANISOU 232 C LEU A 74 8604 6852 8322 -1038 457 852 C ATOM 233 O LEU A 74 214.697 2.919 86.237 1.00 64.42 O ANISOU 233 O LEU A 74 8798 7188 8492 -1058 516 841 O ATOM 234 CB LEU A 74 217.159 1.938 84.335 1.00 59.35 C ANISOU 234 CB LEU A 74 8254 6148 8148 -779 324 795 C ATOM 235 CG LEU A 74 218.526 1.254 84.314 1.00 59.32 C ANISOU 235 CG LEU A 74 8338 5962 8237 -693 173 763 C ATOM 236 CD1 LEU A 74 219.479 2.008 83.404 1.00 58.88 C ANISOU 236 CD1 LEU A 74 8163 5931 8277 -523 224 673 C ATOM 237 CD2 LEU A 74 219.096 1.144 85.717 1.00 59.25 C ANISOU 237 CD2 LEU A 74 8449 5869 8196 -749 87 808 C ATOM 238 N PHE A 75 213.946 2.037 84.307 1.00 63.17 N ANISOU 238 N PHE A 75 8595 7021 8384 -1042 514 828 N ATOM 239 CA PHE A 75 212.737 2.852 84.329 1.00 64.17 C ANISOU 239 CA PHE A 75 8575 7383 8423 -1056 641 776 C ATOM 240 C PHE A 75 211.797 2.429 85.448 1.00 66.38 C ANISOU 240 C PHE A 75 8864 7839 8519 -1284 652 802 C ATOM 241 O PHE A 75 211.109 3.275 86.027 1.00 67.17 O ANISOU 241 O PHE A 75 8839 8152 8530 -1284 742 730 O ATOM 242 CB PHE A 75 212.025 2.773 82.979 1.00 64.69 C ANISOU 242 CB PHE A 75 8554 7507 8519 -1006 686 742 C ATOM 243 CG PHE A 75 210.766 3.591 82.907 1.00 67.52 C ANISOU 243 CG PHE A 75 8754 8106 8795 -988 790 663 C ATOM 244 CD1 PHE A 75 210.821 4.946 82.629 1.00 65.49 C ANISOU 244 CD1 PHE A 75 8404 7881 8599 -800 836 585 C ATOM 245 CD2 PHE A 75 209.527 3.003 83.112 1.00 68.30 C ANISOU 245 CD2 PHE A 75 8800 8405 8746 -1163 822 655 C ATOM 246 CE1 PHE A 75 209.659 5.702 82.559 1.00 67.46 C ANISOU 246 CE1 PHE A 75 8510 8340 8782 -748 895 482 C ATOM 247 CE2 PHE A 75 208.364 3.753 83.045 1.00 67.85 C ANISOU 247 CE2 PHE A 75 8568 8602 8609 -1124 909 544 C ATOM 248 CZ PHE A 75 208.431 5.104 82.768 1.00 68.54 C ANISOU 248 CZ PHE A 75 8564 8702 8777 -897 936 448 C ATOM 249 N VAL A 76 211.752 1.134 85.765 1.00 68.59 N ANISOU 249 N VAL A 76 9292 8043 8726 -1489 546 894 N ATOM 250 CA VAL A 76 210.889 0.662 86.844 1.00 72.36 C ANISOU 250 CA VAL A 76 9796 8707 8991 -1771 543 937 C ATOM 251 C VAL A 76 211.408 1.142 88.194 1.00 74.79 C ANISOU 251 C VAL A 76 10137 9036 9246 -1810 537 947 C ATOM 252 O VAL A 76 210.664 1.721 88.994 1.00 73.66 O ANISOU 252 O VAL A 76 9869 9162 8955 -1902 631 887 O ATOM 253 CB VAL A 76 210.766 -0.872 86.800 1.00 71.71 C ANISOU 253 CB VAL A 76 9912 8497 8839 -2008 389 1055 C ATOM 254 CG1 VAL A 76 210.235 -1.397 88.120 1.00 70.77 C ANISOU 254 CG1 VAL A 76 9882 8519 8487 -2345 341 1135 C ATOM 255 CG2 VAL A 76 209.853 -1.292 85.660 1.00 72.34 C ANISOU 255 CG2 VAL A 76 9922 8659 8904 -2035 427 1035 C ATOM 256 N VAL A 77 212.696 0.914 88.464 1.00 77.22 N ANISOU 256 N VAL A 77 10597 9077 9668 -1733 422 1003 N ATOM 257 CA VAL A 77 213.271 1.298 89.751 1.00 76.37 C ANISOU 257 CA VAL A 77 10538 8965 9514 -1774 402 1023 C ATOM 258 C VAL A 77 213.282 2.814 89.903 1.00 75.77 C ANISOU 258 C VAL A 77 10278 9030 9481 -1577 546 907 C ATOM 259 O VAL A 77 212.906 3.353 90.951 1.00 74.63 O ANISOU 259 O VAL A 77 10067 9077 9213 -1660 605 869 O ATOM 260 CB VAL A 77 214.683 0.706 89.905 1.00 75.11 C ANISOU 260 CB VAL A 77 10574 8483 9480 -1706 231 1089 C ATOM 261 CG1 VAL A 77 215.372 1.296 91.121 1.00 73.93 C ANISOU 261 CG1 VAL A 77 10454 8327 9310 -1701 227 1096 C ATOM 262 CG2 VAL A 77 214.614 -0.809 90.016 1.00 74.73 C ANISOU 262 CG2 VAL A 77 10749 8279 9364 -1923 34 1201 C ATOM 263 N GLY A 78 213.714 3.525 88.859 1.00 75.63 N ANISOU 263 N GLY A 78 10185 8922 9628 -1324 589 845 N ATOM 264 CA GLY A 78 213.788 4.972 88.940 1.00 76.67 C ANISOU 264 CA GLY A 78 10187 9136 9807 -1137 680 745 C ATOM 265 C GLY A 78 212.437 5.642 89.088 1.00 77.10 C ANISOU 265 C GLY A 78 10065 9486 9743 -1151 784 634 C ATOM 266 O GLY A 78 212.336 6.712 89.696 1.00 78.70 O ANISOU 266 O GLY A 78 10179 9799 9924 -1056 829 540 O ATOM 267 N THR A 79 211.383 5.033 88.538 1.00 75.73 N ANISOU 267 N THR A 79 9832 9453 9487 -1258 812 624 N ATOM 268 CA THR A 79 210.051 5.611 88.677 1.00 77.25 C ANISOU 268 CA THR A 79 9830 9969 9552 -1267 902 486 C ATOM 269 C THR A 79 209.569 5.525 90.117 1.00 75.72 C ANISOU 269 C THR A 79 9589 10027 9155 -1473 930 452 C ATOM 270 O THR A 79 209.132 6.525 90.696 1.00 74.01 O ANISOU 270 O THR A 79 9220 10020 8879 -1381 986 301 O ATOM 271 CB THR A 79 209.065 4.910 87.742 1.00 78.89 C ANISOU 271 CB THR A 79 9982 10284 9710 -1352 925 485 C ATOM 272 OG1 THR A 79 209.458 5.127 86.382 1.00 80.68 O ANISOU 272 OG1 THR A 79 10228 10312 10116 -1153 908 497 O ATOM 273 CG2 THR A 79 207.658 5.451 87.945 1.00 80.42 C ANISOU 273 CG2 THR A 79 9950 10855 9751 -1367 1012 315 C ATOM 274 N VAL A 80 209.649 4.336 90.714 1.00 78.05 N ANISOU 274 N VAL A 80 10022 10304 9330 -1761 874 585 N ATOM 275 CA VAL A 80 209.178 4.160 92.084 1.00 80.58 C ANISOU 275 CA VAL A 80 10309 10887 9420 -2020 893 571 C ATOM 276 C VAL A 80 210.070 4.924 93.055 1.00 79.01 C ANISOU 276 C VAL A 80 10141 10611 9267 -1920 883 553 C ATOM 277 O VAL A 80 209.583 5.638 93.940 1.00 75.57 O ANISOU 277 O VAL A 80 9554 10455 8703 -1939 952 421 O ATOM 278 CB VAL A 80 209.107 2.663 92.437 1.00 82.11 C ANISOU 278 CB VAL A 80 10695 11034 9469 -2383 794 747 C ATOM 279 CG1 VAL A 80 208.796 2.476 93.914 1.00 83.80 C ANISOU 279 CG1 VAL A 80 10909 11499 9431 -2691 795 761 C ATOM 280 CG2 VAL A 80 208.072 1.962 91.570 1.00 81.88 C ANISOU 280 CG2 VAL A 80 10615 11135 9358 -2512 813 749 C ATOM 281 N GLY A 81 211.389 4.797 92.895 1.00 81.35 N ANISOU 281 N GLY A 81 10620 10548 9743 -1805 794 666 N ATOM 282 CA GLY A 81 212.305 5.427 93.832 1.00 84.31 C ANISOU 282 CA GLY A 81 11041 10835 10157 -1732 775 665 C ATOM 283 C GLY A 81 212.150 6.934 93.891 1.00 86.77 C ANISOU 283 C GLY A 81 11177 11270 10523 -1480 860 490 C ATOM 284 O GLY A 81 212.108 7.521 94.975 1.00 89.64 O ANISOU 284 O GLY A 81 11476 11790 10793 -1506 890 415 O ATOM 285 N ASN A 82 212.057 7.582 92.729 1.00 82.80 N ANISOU 285 N ASN A 82 10605 10690 10165 -1238 881 422 N ATOM 286 CA ASN A 82 211.900 9.030 92.708 1.00 80.12 C ANISOU 286 CA ASN A 82 10137 10421 9884 -990 913 258 C ATOM 287 C ASN A 82 210.489 9.457 93.091 1.00 78.77 C ANISOU 287 C ASN A 82 9744 10637 9547 -1008 980 62 C ATOM 288 O ASN A 82 210.305 10.556 93.624 1.00 79.91 O ANISOU 288 O ASN A 82 9781 10903 9679 -853 985 -102 O ATOM 289 CB ASN A 82 212.262 9.576 91.328 1.00 82.57 C ANISOU 289 CB ASN A 82 10473 10515 10385 -756 883 261 C ATOM 290 CG ASN A 82 213.735 9.426 91.016 1.00 90.43 C ANISOU 290 CG ASN A 82 11639 11188 11531 -708 822 399 C ATOM 291 OD1 ASN A 82 214.592 9.835 91.799 1.00 93.80 O ANISOU 291 OD1 ASN A 82 12130 11527 11982 -684 797 419 O ATOM 292 ND2 ASN A 82 214.039 8.828 89.870 1.00 94.92 N ANISOU 292 ND2 ASN A 82 12268 11603 12193 -694 798 479 N ATOM 293 N SER A 83 209.488 8.612 92.835 1.00 78.55 N ANISOU 293 N SER A 83 9641 10820 9384 -1191 1020 59 N ATOM 294 CA SER A 83 208.121 8.957 93.208 1.00 80.43 C ANISOU 294 CA SER A 83 9636 11487 9439 -1225 1088 -155 C ATOM 295 C SER A 83 207.925 8.851 94.714 1.00 84.40 C ANISOU 295 C SER A 83 10072 12272 9724 -1446 1125 -207 C ATOM 296 O SER A 83 207.386 9.767 95.344 1.00 85.98 O ANISOU 296 O SER A 83 10078 12749 9840 -1336 1157 -433 O ATOM 297 CB SER A 83 207.129 8.058 92.472 1.00 78.56 C ANISOU 297 CB SER A 83 9333 11412 9103 -1385 1124 -138 C ATOM 298 OG SER A 83 207.322 8.135 91.071 1.00 78.15 O ANISOU 298 OG SER A 83 9342 11107 9246 -1192 1091 -88 O ATOM 299 N VAL A 84 208.358 7.734 95.306 1.00 87.36 N ANISOU 299 N VAL A 84 10611 12583 10000 -1759 1103 -9 N ATOM 300 CA VAL A 84 208.249 7.562 96.753 1.00 89.21 C ANISOU 300 CA VAL A 84 10813 13072 10010 -2017 1125 -26 C ATOM 301 C VAL A 84 208.983 8.682 97.478 1.00 91.53 C ANISOU 301 C VAL A 84 11092 13291 10394 -1800 1116 -117 C ATOM 302 O VAL A 84 208.484 9.234 98.467 1.00 94.19 O ANISOU 302 O VAL A 84 11254 13966 10566 -1842 1167 -294 O ATOM 303 CB VAL A 84 208.776 6.175 97.168 1.00 87.32 C ANISOU 303 CB VAL A 84 10823 12668 9684 -2372 1048 238 C ATOM 304 CG1 VAL A 84 208.868 6.068 98.682 1.00 86.85 C ANISOU 304 CG1 VAL A 84 10774 12816 9410 -2638 1049 249 C ATOM 305 CG2 VAL A 84 207.880 5.080 96.609 1.00 86.29 C ANISOU 305 CG2 VAL A 84 10699 12673 9414 -2634 1048 307 C ATOM 306 N THR A 85 210.171 9.047 96.992 1.00 90.54 N ANISOU 306 N THR A 85 11138 12743 10519 -1574 1050 -10 N ATOM 307 CA THR A 85 210.894 10.170 97.579 1.00 91.21 C ANISOU 307 CA THR A 85 11223 12734 10700 -1361 1032 -91 C ATOM 308 C THR A 85 210.130 11.474 97.385 1.00 94.14 C ANISOU 308 C THR A 85 11376 13303 11090 -1079 1053 -366 C ATOM 309 O THR A 85 210.078 12.314 98.291 1.00 98.20 O ANISOU 309 O THR A 85 11788 13978 11546 -996 1058 -528 O ATOM 310 CB THR A 85 212.293 10.272 96.970 1.00 91.95 C ANISOU 310 CB THR A 85 11532 12365 11039 -1198 956 75 C ATOM 311 OG1 THR A 85 213.012 9.056 97.214 1.00 94.93 O ANISOU 311 OG1 THR A 85 12107 12561 11400 -1428 904 295 O ATOM 312 CG2 THR A 85 213.061 11.436 97.582 1.00 87.69 C ANISOU 312 CG2 THR A 85 11006 11726 10586 -1004 930 3 C ATOM 313 N LEU A 86 209.515 11.654 96.214 1.00 89.90 N ANISOU 313 N LEU A 86 10769 12755 10634 -921 1048 -434 N ATOM 314 CA LEU A 86 208.770 12.878 95.947 1.00 88.23 C ANISOU 314 CA LEU A 86 10373 12697 10453 -627 1023 -705 C ATOM 315 C LEU A 86 207.395 12.867 96.606 1.00 97.25 C ANISOU 315 C LEU A 86 11232 14370 11349 -724 1092 -957 C ATOM 316 O LEU A 86 206.899 13.926 97.007 1.00103.26 O ANISOU 316 O LEU A 86 11818 15335 12083 -506 1060 -1233 O ATOM 317 CB LEU A 86 208.633 13.091 94.438 1.00 82.78 C ANISOU 317 CB LEU A 86 9725 11794 9936 -426 971 -683 C ATOM 318 CG LEU A 86 208.011 14.404 93.963 1.00 83.47 C ANISOU 318 CG LEU A 86 9689 11927 10099 -85 886 -935 C ATOM 319 CD1 LEU A 86 208.839 15.593 94.424 1.00 84.26 C ANISOU 319 CD1 LEU A 86 9884 11817 10315 130 786 -987 C ATOM 320 CD2 LEU A 86 207.853 14.407 92.450 1.00 83.27 C ANISOU 320 CD2 LEU A 86 9725 11699 10215 43 835 -874 C ATOM 321 N PHE A 87 206.773 11.693 96.735 1.00101.06 N ANISOU 321 N PHE A 87 11663 15096 11638 -1054 1171 -882 N ATOM 322 CA PHE A 87 205.433 11.628 97.312 1.00104.02 C ANISOU 322 CA PHE A 87 11745 16036 11744 -1191 1247 -1129 C ATOM 323 C PHE A 87 205.470 11.837 98.820 1.00104.89 C ANISOU 323 C PHE A 87 11755 16441 11657 -1344 1286 -1237 C ATOM 324 O PHE A 87 204.742 12.680 99.358 1.00109.27 O ANISOU 324 O PHE A 87 12047 17368 12102 -1200 1298 -1560 O ATOM 325 CB PHE A 87 204.778 10.288 96.974 1.00105.43 C ANISOU 325 CB PHE A 87 11920 16384 11753 -1544 1310 -995 C ATOM 326 CG PHE A 87 203.457 10.068 97.655 1.00106.63 C ANISOU 326 CG PHE A 87 11771 17167 11575 -1777 1400 -1224 C ATOM 327 CD1 PHE A 87 202.303 10.661 97.167 1.00110.42 C ANISOU 327 CD1 PHE A 87 11963 17983 12008 -1574 1419 -1531 C ATOM 328 CD2 PHE A 87 203.367 9.263 98.779 1.00108.88 C ANISOU 328 CD2 PHE A 87 12059 17727 11582 -2214 1454 -1139 C ATOM 329 CE1 PHE A 87 201.084 10.458 97.790 1.00115.25 C ANISOU 329 CE1 PHE A 87 12263 19232 12295 -1794 1507 -1772 C ATOM 330 CE2 PHE A 87 202.153 9.057 99.408 1.00114.05 C ANISOU 330 CE2 PHE A 87 12421 19016 11898 -2473 1543 -1356 C ATOM 331 CZ PHE A 87 201.010 9.655 98.912 1.00117.13 C ANISOU 331 CZ PHE A 87 12492 19774 12238 -2260 1578 -1684 C ATOM 332 N THR A 88 206.310 11.074 99.521 1.00100.89 N ANISOU 332 N THR A 88 11454 15781 11100 -1630 1291 -984 N ATOM 333 CA THR A 88 206.367 11.158 100.974 1.00100.45 C ANISOU 333 CA THR A 88 11323 16009 10836 -1829 1328 -1055 C ATOM 334 C THR A 88 206.899 12.495 101.471 1.00103.87 C ANISOU 334 C THR A 88 11714 16352 11401 -1493 1282 -1230 C ATOM 335 O THR A 88 206.758 12.790 102.663 1.00106.62 O ANISOU 335 O THR A 88 11930 17013 11568 -1597 1318 -1374 O ATOM 336 CB THR A 88 207.226 10.023 101.535 1.00 98.50 C ANISOU 336 CB THR A 88 11351 15548 10527 -2197 1305 -720 C ATOM 337 OG1 THR A 88 208.561 10.135 101.027 1.00 94.15 O ANISOU 337 OG1 THR A 88 11076 14425 10273 -1995 1218 -509 O ATOM 338 CG2 THR A 88 206.648 8.672 101.138 1.00100.87 C ANISOU 338 CG2 THR A 88 11713 15943 10669 -2561 1318 -553 C ATOM 339 N LEU A 89 207.498 13.308 100.597 1.00103.58 N ANISOU 339 N LEU A 89 11791 15908 11657 -1115 1197 -1221 N ATOM 340 CA LEU A 89 208.017 14.602 101.028 1.00102.36 C ANISOU 340 CA LEU A 89 11629 15635 11628 -805 1125 -1376 C ATOM 341 C LEU A 89 206.886 15.549 101.413 1.00108.91 C ANISOU 341 C LEU A 89 12134 16911 12335 -601 1119 -1793 C ATOM 342 O LEU A 89 206.943 16.206 102.459 1.00115.20 O ANISOU 342 O LEU A 89 12825 17897 13049 -547 1111 -1977 O ATOM 343 CB LEU A 89 208.884 15.218 99.930 1.00 98.30 C ANISOU 343 CB LEU A 89 11329 14592 11428 -497 1017 -1255 C ATOM 344 CG LEU A 89 209.423 16.614 100.245 1.00 95.01 C ANISOU 344 CG LEU A 89 10943 14007 11149 -176 911 -1402 C ATOM 345 CD1 LEU A 89 210.186 16.606 101.559 1.00 96.79 C ANISOU 345 CD1 LEU A 89 11226 14254 11296 -326 940 -1343 C ATOM 346 CD2 LEU A 89 210.302 17.123 99.114 1.00 93.17 C ANISOU 346 CD2 LEU A 89 10943 13268 11188 48 801 -1246 C ATOM 347 N ALA A 90 205.849 15.633 100.579 1.00109.08 N ANISOU 347 N ALA A 90 11987 17115 12343 -473 1111 -1967 N ATOM 348 CA ALA A 90 204.719 16.511 100.856 1.00114.10 C ANISOU 348 CA ALA A 90 12294 18192 12868 -242 1080 -2404 C ATOM 349 C ALA A 90 203.989 16.077 102.121 1.00119.75 C ANISOU 349 C ALA A 90 12736 19530 13233 -553 1205 -2586 C ATOM 350 O ALA A 90 203.267 15.074 102.117 1.00125.11 O ANISOU 350 O ALA A 90 13299 20548 13691 -890 1316 -2543 O ATOM 351 CB ALA A 90 203.757 16.537 99.666 1.00115.84 C ANISOU 351 CB ALA A 90 12393 18488 13133 -74 1045 -2534 C ATOM 352 N ARG A 91 204.169 16.826 103.205 1.00121.46 N ANISOU 352 N ARG A 91 12850 19914 13383 -464 1183 -2788 N ATOM 353 CA ARG A 91 203.551 16.489 104.483 1.00123.70 C ANISOU 353 CA ARG A 91 12867 20816 13316 -775 1301 -2972 C ATOM 354 C ARG A 91 203.306 17.734 105.330 1.00127.03 C ANISOU 354 C ARG A 91 13055 21513 13699 -472 1232 -3390 C ATOM 355 O ARG A 91 203.975 18.754 105.161 1.00127.60 O ANISOU 355 O ARG A 91 13273 21182 14027 -94 1089 -3431 O ATOM 356 CB ARG A 91 204.425 15.493 105.247 1.00123.05 C ANISOU 356 CB ARG A 91 13015 20610 13129 -1227 1384 -2598 C ATOM 357 CG ARG A 91 205.816 16.014 105.572 1.00123.54 C ANISOU 357 CG ARG A 91 13360 20160 13421 -1074 1304 -2411 C ATOM 358 CD ARG A 91 206.706 14.915 106.128 1.00121.88 C ANISOU 358 CD ARG A 91 13411 19761 13138 -1499 1357 -2016 C ATOM 359 NE ARG A 91 208.030 15.415 106.487 1.00121.46 N ANISOU 359 NE ARG A 91 13602 19261 13288 -1357 1285 -1860 N ATOM 360 CZ ARG A 91 209.035 14.646 106.893 1.00119.26 C ANISOU 360 CZ ARG A 91 13589 18704 13019 -1624 1286 -1524 C ATOM 361 NH1 ARG A 91 208.868 13.334 106.994 1.00120.34 N ANISOU 361 NH1 ARG A 91 13810 18934 12979 -2047 1333 -1298 N ATOM 362 NH2 ARG A 91 210.208 15.188 107.196 1.00117.26 N ANISOU 362 NH2 ARG A 91 13528 18077 12949 -1467 1221 -1417 N ATOM 363 N SER A 100 214.859 22.372 109.198 1.00114.70 N ANISOU 363 N SER A 100 13700 16307 13572 236 623 -1934 N ATOM 364 CA SER A 100 215.698 21.447 108.445 1.00113.19 C ANISOU 364 CA SER A 100 13742 15773 13492 56 663 -1552 C ATOM 365 C SER A 100 215.248 21.381 106.989 1.00111.31 C ANISOU 365 C SER A 100 13533 15377 13381 194 617 -1524 C ATOM 366 O SER A 100 214.464 20.509 106.611 1.00113.44 O ANISOU 366 O SER A 100 13693 15858 13552 46 703 -1507 O ATOM 367 CB SER A 100 215.662 20.054 109.079 1.00110.25 C ANISOU 367 CB SER A 100 13344 15621 12927 -348 807 -1372 C ATOM 368 OG SER A 100 216.272 19.095 108.234 1.00108.83 O ANISOU 368 OG SER A 100 13361 15139 12851 -486 822 -1055 O ATOM 369 N THR A 101 215.752 22.306 106.173 1.00108.71 N ANISOU 369 N THR A 101 13365 14680 13262 457 474 -1510 N ATOM 370 CA THR A 101 215.310 22.461 104.795 1.00107.18 C ANISOU 370 CA THR A 101 13205 14329 13189 617 399 -1511 C ATOM 371 C THR A 101 216.164 21.672 103.807 1.00107.14 C ANISOU 371 C THR A 101 13406 13998 13304 474 435 -1168 C ATOM 372 O THR A 101 216.256 22.062 102.636 1.00108.54 O ANISOU 372 O THR A 101 13693 13924 13624 619 339 -1119 O ATOM 373 CB THR A 101 215.315 23.940 104.408 1.00106.58 C ANISOU 373 CB THR A 101 13207 14037 13254 965 186 -1693 C ATOM 374 OG1 THR A 101 216.668 24.400 104.299 1.00103.81 O ANISOU 374 OG1 THR A 101 13120 13284 13040 966 109 -1482 O ATOM 375 CG2 THR A 101 214.601 24.766 105.464 1.00110.17 C ANISOU 375 CG2 THR A 101 13463 14796 13600 1139 123 -2060 C ATOM 376 N VAL A 102 216.790 20.576 104.247 1.00106.29 N ANISOU 376 N VAL A 102 13355 13893 13135 195 553 -943 N ATOM 377 CA VAL A 102 217.659 19.804 103.361 1.00105.65 C ANISOU 377 CA VAL A 102 13455 13518 13168 81 570 -654 C ATOM 378 C VAL A 102 216.897 18.845 102.463 1.00108.51 C ANISOU 378 C VAL A 102 13754 13971 13503 -11 631 -600 C ATOM 379 O VAL A 102 217.510 18.212 101.594 1.00108.60 O ANISOU 379 O VAL A 102 13896 13754 13612 -76 634 -393 O ATOM 380 CB VAL A 102 218.706 19.012 104.166 1.00103.43 C ANISOU 380 CB VAL A 102 13284 13166 12851 -148 628 -448 C ATOM 381 CG1 VAL A 102 219.366 19.910 105.198 1.00101.41 C ANISOU 381 CG1 VAL A 102 13066 12872 12594 -81 583 -516 C ATOM 382 CG2 VAL A 102 218.057 17.813 104.838 1.00103.40 C ANISOU 382 CG2 VAL A 102 13177 13454 12657 -418 731 -421 C ATOM 383 N HIS A 103 215.581 18.712 102.646 1.00111.36 N ANISOU 383 N HIS A 103 13907 14681 13726 -20 677 -794 N ATOM 384 CA HIS A 103 214.793 17.877 101.747 1.00112.99 C ANISOU 384 CA HIS A 103 14048 14980 13903 -100 728 -756 C ATOM 385 C HIS A 103 214.368 18.634 100.498 1.00111.71 C ANISOU 385 C HIS A 103 13885 14681 13877 163 634 -851 C ATOM 386 O HIS A 103 214.192 18.020 99.439 1.00112.40 O ANISOU 386 O HIS A 103 14008 14682 14018 123 652 -738 O ATOM 387 CB HIS A 103 213.553 17.340 102.460 1.00115.09 C ANISOU 387 CB HIS A 103 14080 15717 13933 -265 822 -920 C ATOM 388 CG HIS A 103 213.724 17.174 103.935 1.00119.01 C ANISOU 388 CG HIS A 103 14525 16434 14259 -455 877 -949 C ATOM 389 ND1 HIS A 103 214.612 16.274 104.484 1.00120.37 N ANISOU 389 ND1 HIS A 103 14858 16479 14397 -716 908 -697 N ATOM 390 CD2 HIS A 103 213.115 17.786 104.978 1.00122.81 C ANISOU 390 CD2 HIS A 103 14808 17268 14586 -424 894 -1210 C ATOM 391 CE1 HIS A 103 214.546 16.343 105.802 1.00123.44 C ANISOU 391 CE1 HIS A 103 15164 17121 14615 -857 945 -781 C ATOM 392 NE2 HIS A 103 213.644 17.253 106.127 1.00124.85 N ANISOU 392 NE2 HIS A 103 15116 17609 14713 -688 948 -1095 N ATOM 393 N TYR A 104 214.191 19.953 100.610 1.00109.04 N ANISOU 393 N TYR A 104 13521 14316 13595 429 515 -1060 N ATOM 394 CA TYR A 104 213.805 20.762 99.459 1.00105.90 C ANISOU 394 CA TYR A 104 13158 13755 13323 683 379 -1150 C ATOM 395 C TYR A 104 214.772 20.572 98.298 1.00106.05 C ANISOU 395 C TYR A 104 13404 13390 13500 647 344 -879 C ATOM 396 O TYR A 104 214.365 20.569 97.130 1.00107.94 O ANISOU 396 O TYR A 104 13662 13545 13807 722 298 -863 O ATOM 397 CB TYR A 104 213.729 22.234 99.864 1.00104.48 C ANISOU 397 CB TYR A 104 12986 13522 13191 964 206 -1385 C ATOM 398 CG TYR A 104 212.462 22.615 100.594 1.00106.49 C ANISOU 398 CG TYR A 104 12969 14185 13307 1100 192 -1748 C ATOM 399 CD1 TYR A 104 212.134 22.033 101.812 1.00108.71 C ANISOU 399 CD1 TYR A 104 13060 14849 13396 913 341 -1835 C ATOM 400 CD2 TYR A 104 211.597 23.564 100.068 1.00108.95 C ANISOU 400 CD2 TYR A 104 13212 14516 13669 1411 15 -2018 C ATOM 401 CE1 TYR A 104 210.975 22.383 102.482 1.00110.77 C ANISOU 401 CE1 TYR A 104 13038 15547 13504 1023 336 -2197 C ATOM 402 CE2 TYR A 104 210.438 23.920 100.730 1.00111.17 C ANISOU 402 CE2 TYR A 104 13213 15209 13818 1561 -8 -2395 C ATOM 403 CZ TYR A 104 210.132 23.328 101.935 1.00114.56 C ANISOU 403 CZ TYR A 104 13426 16059 14044 1361 164 -2491 C ATOM 404 OH TYR A 104 208.978 23.683 102.594 1.00118.56 O ANISOU 404 OH TYR A 104 13620 17034 14393 1496 149 -2894 O ATOM 405 N HIS A 105 216.061 20.406 98.599 1.00104.66 N ANISOU 405 N HIS A 105 13389 13003 13374 529 365 -677 N ATOM 406 CA HIS A 105 217.014 20.052 97.556 1.00101.01 C ANISOU 406 CA HIS A 105 13100 12251 13028 457 356 -437 C ATOM 407 C HIS A 105 216.840 18.601 97.127 1.00100.50 C ANISOU 407 C HIS A 105 12991 12271 12925 262 482 -298 C ATOM 408 O HIS A 105 216.877 18.294 95.930 1.00106.10 O ANISOU 408 O HIS A 105 13749 12857 13707 263 472 -203 O ATOM 409 CB HIS A 105 218.441 20.307 98.040 1.00100.30 C ANISOU 409 CB HIS A 105 13167 11953 12990 396 335 -296 C ATOM 410 CG HIS A 105 218.707 21.733 98.406 1.00104.08 C ANISOU 410 CG HIS A 105 13725 12310 13509 568 192 -409 C ATOM 411 ND1 HIS A 105 218.775 22.165 99.713 1.00107.76 N ANISOU 411 ND1 HIS A 105 14148 12885 13912 593 190 -524 N ATOM 412 CD2 HIS A 105 218.921 22.826 97.636 1.00106.90 C ANISOU 412 CD2 HIS A 105 14221 12438 13957 712 25 -422 C ATOM 413 CE1 HIS A 105 219.020 23.464 99.732 1.00110.38 C ANISOU 413 CE1 HIS A 105 14586 13049 14303 764 26 -612 C ATOM 414 NE2 HIS A 105 219.112 23.889 98.484 1.00109.75 N ANISOU 414 NE2 HIS A 105 14631 12754 14315 830 -86 -546 N ATOM 415 N LEU A 106 216.640 17.696 98.090 1.00 92.44 N ANISOU 415 N LEU A 106 11888 11455 11779 81 587 -283 N ATOM 416 CA LEU A 106 216.447 16.290 97.750 1.00 88.60 C ANISOU 416 CA LEU A 106 11390 11030 11245 -120 672 -150 C ATOM 417 C LEU A 106 215.173 16.090 96.942 1.00 89.06 C ANISOU 417 C LEU A 106 11318 11254 11265 -79 693 -251 C ATOM 418 O LEU A 106 215.152 15.306 95.986 1.00 88.55 O ANISOU 418 O LEU A 106 11292 11109 11244 -147 714 -133 O ATOM 419 CB LEU A 106 216.417 15.440 99.021 1.00 87.83 C ANISOU 419 CB LEU A 106 11258 11118 10994 -349 744 -114 C ATOM 420 CG LEU A 106 216.108 13.951 98.837 1.00 88.04 C ANISOU 420 CG LEU A 106 11296 11216 10939 -589 797 18 C ATOM 421 CD1 LEU A 106 217.106 13.298 97.894 1.00 86.64 C ANISOU 421 CD1 LEU A 106 11282 10730 10905 -600 757 212 C ATOM 422 CD2 LEU A 106 216.085 13.238 100.180 1.00 89.72 C ANISOU 422 CD2 LEU A 106 11508 11605 10978 -841 831 59 C ATOM 423 N GLY A 107 214.099 16.792 97.310 1.00 91.54 N ANISOU 423 N GLY A 107 11466 11816 11498 41 680 -488 N ATOM 424 CA GLY A 107 212.873 16.699 96.536 1.00 93.23 C ANISOU 424 CA GLY A 107 11540 12205 11677 106 687 -614 C ATOM 425 C GLY A 107 213.024 17.278 95.144 1.00 91.79 C ANISOU 425 C GLY A 107 11457 11759 11660 295 588 -579 C ATOM 426 O GLY A 107 212.444 16.767 94.182 1.00 93.07 O ANISOU 426 O GLY A 107 11581 11949 11832 276 609 -553 O ATOM 427 N SER A 108 213.805 18.354 95.016 1.00 88.24 N ANISOU 427 N SER A 108 11145 11056 11329 455 469 -572 N ATOM 428 CA SER A 108 214.083 18.910 93.698 1.00 85.81 C ANISOU 428 CA SER A 108 10967 10482 11156 580 358 -506 C ATOM 429 C SER A 108 214.853 17.916 92.840 1.00 83.20 C ANISOU 429 C SER A 108 10738 9991 10882 410 429 -261 C ATOM 430 O SER A 108 214.548 17.740 91.654 1.00 82.02 O ANISOU 430 O SER A 108 10602 9780 10781 433 409 -220 O ATOM 431 CB SER A 108 214.859 20.219 93.835 1.00 90.14 C ANISOU 431 CB SER A 108 11669 10790 11790 727 204 -523 C ATOM 432 OG SER A 108 215.199 20.748 92.566 1.00 93.03 O ANISOU 432 OG SER A 108 12187 10900 12261 793 83 -432 O ATOM 433 N LEU A 109 215.853 17.252 93.424 1.00 82.40 N ANISOU 433 N LEU A 109 10707 9829 10774 250 499 -114 N ATOM 434 CA LEU A 109 216.593 16.232 92.690 1.00 79.62 C ANISOU 434 CA LEU A 109 10433 9349 10471 109 549 79 C ATOM 435 C LEU A 109 215.697 15.052 92.332 1.00 81.35 C ANISOU 435 C LEU A 109 10553 9729 10625 -2 631 90 C ATOM 436 O LEU A 109 215.810 14.490 91.237 1.00 77.75 O ANISOU 436 O LEU A 109 10131 9185 10225 -33 638 181 O ATOM 437 CB LEU A 109 217.797 15.768 93.509 1.00 77.46 C ANISOU 437 CB LEU A 109 10245 8989 10198 -13 577 197 C ATOM 438 CG LEU A 109 218.687 14.703 92.865 1.00 76.36 C ANISOU 438 CG LEU A 109 10181 8721 10112 -128 600 359 C ATOM 439 CD1 LEU A 109 219.313 15.237 91.589 1.00 81.23 C ANISOU 439 CD1 LEU A 109 10866 9171 10827 -58 545 408 C ATOM 440 CD2 LEU A 109 219.761 14.222 93.830 1.00 75.56 C ANISOU 440 CD2 LEU A 109 10150 8558 10000 -227 605 440 C ATOM 441 N ALA A 110 214.793 14.670 93.237 1.00 83.42 N ANISOU 441 N ALA A 110 10691 10249 10755 -79 691 -7 N ATOM 442 CA ALA A 110 213.905 13.544 92.968 1.00 82.27 C ANISOU 442 CA ALA A 110 10460 10278 10520 -224 763 9 C ATOM 443 C ALA A 110 212.977 13.826 91.796 1.00 83.10 C ANISOU 443 C ALA A 110 10485 10430 10659 -101 744 -76 C ATOM 444 O ALA A 110 212.564 12.896 91.093 1.00 81.92 O ANISOU 444 O ALA A 110 10318 10316 10493 -203 786 -11 O ATOM 445 CB ALA A 110 213.092 13.205 94.218 1.00 85.81 C ANISOU 445 CB ALA A 110 10779 11041 10782 -366 826 -92 C ATOM 446 N LEU A 111 212.638 15.096 91.568 1.00 83.97 N ANISOU 446 N LEU A 111 10562 10527 10817 120 662 -224 N ATOM 447 CA LEU A 111 211.770 15.445 90.450 1.00 83.70 C ANISOU 447 CA LEU A 111 10468 10516 10820 256 613 -311 C ATOM 448 C LEU A 111 212.518 15.381 89.125 1.00 82.99 C ANISOU 448 C LEU A 111 10524 10149 10860 266 569 -146 C ATOM 449 O LEU A 111 212.009 14.827 88.144 1.00 86.61 O ANISOU 449 O LEU A 111 10948 10631 11327 238 594 -115 O ATOM 450 CB LEU A 111 211.177 16.840 90.661 1.00 84.07 C ANISOU 450 CB LEU A 111 10454 10612 10876 506 491 -537 C ATOM 451 CG LEU A 111 210.393 17.420 89.482 1.00 83.56 C ANISOU 451 CG LEU A 111 10368 10511 10871 689 383 -634 C ATOM 452 CD1 LEU A 111 209.170 16.570 89.187 1.00 84.33 C ANISOU 452 CD1 LEU A 111 10277 10896 10868 620 478 -716 C ATOM 453 CD2 LEU A 111 209.997 18.860 89.754 1.00 83.32 C ANISOU 453 CD2 LEU A 111 10328 10461 10868 960 205 -858 C ATOM 454 N SER A 112 213.731 15.940 89.080 1.00 80.38 N ANISOU 454 N SER A 112 10346 9579 10616 290 507 -47 N ATOM 455 CA SER A 112 214.469 16.006 87.823 1.00 77.33 C ANISOU 455 CA SER A 112 10081 8975 10325 282 461 87 C ATOM 456 C SER A 112 214.868 14.623 87.326 1.00 75.90 C ANISOU 456 C SER A 112 9901 8788 10149 116 558 226 C ATOM 457 O SER A 112 214.892 14.388 86.114 1.00 74.24 O ANISOU 457 O SER A 112 9712 8511 9984 106 548 284 O ATOM 458 CB SER A 112 215.703 16.893 87.983 1.00 75.03 C ANISOU 458 CB SER A 112 9939 8477 10092 306 377 154 C ATOM 459 OG SER A 112 216.649 16.302 88.854 1.00 74.12 O ANISOU 459 OG SER A 112 9850 8350 9963 188 449 236 O ATOM 460 N ASP A 113 215.183 13.698 88.235 1.00 78.72 N ANISOU 460 N ASP A 113 10246 9206 10457 -14 633 274 N ATOM 461 CA ASP A 113 215.503 12.340 87.808 1.00 86.63 C ANISOU 461 CA ASP A 113 11269 10183 11466 -154 684 385 C ATOM 462 C ASP A 113 214.278 11.628 87.248 1.00 88.56 C ANISOU 462 C ASP A 113 11417 10575 11656 -198 728 351 C ATOM 463 O ASP A 113 214.407 10.800 86.338 1.00 91.25 O ANISOU 463 O ASP A 113 11778 10858 12032 -256 739 424 O ATOM 464 CB ASP A 113 216.097 11.538 88.968 1.00 97.05 C ANISOU 464 CB ASP A 113 12630 11504 12738 -284 708 445 C ATOM 465 CG ASP A 113 217.488 12.012 89.359 1.00103.24 C ANISOU 465 CG ASP A 113 13512 12130 13585 -256 666 497 C ATOM 466 OD1 ASP A 113 218.428 11.833 88.555 1.00104.60 O ANISOU 466 OD1 ASP A 113 13739 12169 13833 -250 640 562 O ATOM 467 OD2 ASP A 113 217.647 12.544 90.477 1.00107.20 O ANISOU 467 OD2 ASP A 113 14021 12662 14047 -246 662 461 O ATOM 468 N LEU A 114 213.088 11.934 87.771 1.00 86.42 N ANISOU 468 N LEU A 114 11029 10515 11294 -172 751 223 N ATOM 469 CA LEU A 114 211.877 11.304 87.256 1.00 79.58 C ANISOU 469 CA LEU A 114 10054 9825 10358 -224 796 176 C ATOM 470 C LEU A 114 211.504 11.864 85.888 1.00 79.61 C ANISOU 470 C LEU A 114 10042 9764 10442 -82 751 143 C ATOM 471 O LEU A 114 211.046 11.122 85.011 1.00 79.55 O ANISOU 471 O LEU A 114 10006 9786 10433 -140 780 180 O ATOM 472 CB LEU A 114 210.728 11.487 88.249 1.00 80.70 C ANISOU 472 CB LEU A 114 10041 10267 10352 -247 835 18 C ATOM 473 CG LEU A 114 209.378 10.870 87.872 1.00 81.05 C ANISOU 473 CG LEU A 114 9942 10565 10289 -325 889 -58 C ATOM 474 CD1 LEU A 114 209.475 9.353 87.769 1.00 78.99 C ANISOU 474 CD1 LEU A 114 9748 10292 9974 -575 935 98 C ATOM 475 CD2 LEU A 114 208.314 11.271 88.877 1.00 82.54 C ANISOU 475 CD2 LEU A 114 9943 11101 10317 -326 923 -261 C ATOM 476 N LEU A 115 211.701 13.170 85.684 1.00 79.43 N ANISOU 476 N LEU A 115 10056 9641 10485 94 661 80 N ATOM 477 CA LEU A 115 211.391 13.771 84.391 1.00 77.74 C ANISOU 477 CA LEU A 115 9861 9339 10337 212 584 63 C ATOM 478 C LEU A 115 212.284 13.220 83.288 1.00 74.47 C ANISOU 478 C LEU A 115 9546 8754 9997 124 594 224 C ATOM 479 O LEU A 115 211.853 13.116 82.134 1.00 74.62 O ANISOU 479 O LEU A 115 9550 8763 10039 142 578 236 O ATOM 480 CB LEU A 115 211.526 15.291 84.472 1.00 76.90 C ANISOU 480 CB LEU A 115 9823 9119 10278 395 442 -21 C ATOM 481 CG LEU A 115 210.587 16.001 85.448 1.00 79.44 C ANISOU 481 CG LEU A 115 10030 9619 10535 538 398 -234 C ATOM 482 CD1 LEU A 115 210.915 17.482 85.527 1.00 79.99 C ANISOU 482 CD1 LEU A 115 10214 9511 10666 722 218 -304 C ATOM 483 CD2 LEU A 115 209.138 15.794 85.049 1.00 80.80 C ANISOU 483 CD2 LEU A 115 10035 10019 10648 605 409 -385 C ATOM 484 N ILE A 116 213.527 12.865 83.621 1.00 72.58 N ANISOU 484 N ILE A 116 9393 8398 9787 35 615 331 N ATOM 485 CA ILE A 116 214.431 12.281 82.633 1.00 68.68 C ANISOU 485 CA ILE A 116 8958 7789 9348 -42 624 444 C ATOM 486 C ILE A 116 213.905 10.932 82.163 1.00 68.93 C ANISOU 486 C ILE A 116 8929 7903 9360 -135 693 469 C ATOM 487 O ILE A 116 213.968 10.602 80.972 1.00 68.33 O ANISOU 487 O ILE A 116 8850 7793 9317 -151 691 505 O ATOM 488 CB ILE A 116 215.851 12.165 83.219 1.00 65.11 C ANISOU 488 CB ILE A 116 8585 7232 8923 -99 623 514 C ATOM 489 CG1 ILE A 116 216.462 13.553 83.412 1.00 66.02 C ANISOU 489 CG1 ILE A 116 8781 7246 9057 -30 542 507 C ATOM 490 CG2 ILE A 116 216.736 11.306 82.335 1.00 62.64 C ANISOU 490 CG2 ILE A 116 8290 6862 8650 -177 638 585 C ATOM 491 CD1 ILE A 116 217.829 13.530 84.050 1.00 68.59 C ANISOU 491 CD1 ILE A 116 9170 7493 9397 -85 542 562 C ATOM 492 N LEU A 117 213.363 10.138 83.086 1.00 70.15 N ANISOU 492 N LEU A 117 9037 8171 9444 -215 744 451 N ATOM 493 CA LEU A 117 212.874 8.813 82.726 1.00 69.78 C ANISOU 493 CA LEU A 117 8964 8186 9365 -331 784 487 C ATOM 494 C LEU A 117 211.564 8.880 81.955 1.00 73.68 C ANISOU 494 C LEU A 117 9358 8816 9823 -300 807 421 C ATOM 495 O LEU A 117 211.285 7.997 81.137 1.00 77.63 O ANISOU 495 O LEU A 117 9847 9323 10327 -367 825 459 O ATOM 496 CB LEU A 117 212.706 7.966 83.985 1.00 71.39 C ANISOU 496 CB LEU A 117 9180 8467 9477 -473 806 505 C ATOM 497 CG LEU A 117 214.005 7.640 84.717 1.00 70.23 C ANISOU 497 CG LEU A 117 9146 8172 9366 -515 766 577 C ATOM 498 CD1 LEU A 117 213.705 7.082 86.090 1.00 69.72 C ANISOU 498 CD1 LEU A 117 9102 8199 9188 -661 772 592 C ATOM 499 CD2 LEU A 117 214.820 6.652 83.902 1.00 69.01 C ANISOU 499 CD2 LEU A 117 9063 7871 9287 -543 722 644 C ATOM 500 N LEU A 118 210.753 9.908 82.193 1.00 74.13 N ANISOU 500 N LEU A 118 9337 8982 9846 -188 792 309 N ATOM 501 CA LEU A 118 209.443 9.987 81.561 1.00 77.16 C ANISOU 501 CA LEU A 118 9607 9524 10187 -142 802 217 C ATOM 502 C LEU A 118 209.470 10.689 80.213 1.00 79.78 C ANISOU 502 C LEU A 118 9970 9740 10605 -20 734 222 C ATOM 503 O LEU A 118 208.621 10.403 79.360 1.00 81.10 O ANISOU 503 O LEU A 118 10068 9988 10756 -14 745 193 O ATOM 504 CB LEU A 118 208.454 10.707 82.482 1.00 78.89 C ANISOU 504 CB LEU A 118 9702 9957 10316 -60 797 49 C ATOM 505 CG LEU A 118 208.162 10.022 83.818 1.00 79.73 C ANISOU 505 CG LEU A 118 9747 10258 10290 -221 871 25 C ATOM 506 CD1 LEU A 118 207.129 10.809 84.609 1.00 80.96 C ANISOU 506 CD1 LEU A 118 9738 10682 10342 -125 868 -187 C ATOM 507 CD2 LEU A 118 207.704 8.587 83.598 1.00 83.52 C ANISOU 507 CD2 LEU A 118 10210 10834 10688 -437 938 104 C ATOM 508 N LEU A 119 210.421 11.595 79.994 1.00 81.09 N ANISOU 508 N LEU A 119 10243 9722 10844 55 657 264 N ATOM 509 CA LEU A 119 210.433 12.426 78.796 1.00 83.74 C ANISOU 509 CA LEU A 119 10635 9949 11235 142 562 274 C ATOM 510 C LEU A 119 211.480 11.988 77.780 1.00 81.58 C ANISOU 510 C LEU A 119 10439 9548 11009 39 573 405 C ATOM 511 O LEU A 119 211.158 11.791 76.605 1.00 84.91 O ANISOU 511 O LEU A 119 10846 9974 11440 23 565 428 O ATOM 512 CB LEU A 119 210.661 13.893 79.184 1.00 85.20 C ANISOU 512 CB LEU A 119 10902 10027 11442 277 429 221 C ATOM 513 CG LEU A 119 209.580 14.532 80.060 1.00 88.39 C ANISOU 513 CG LEU A 119 11213 10569 11802 429 382 39 C ATOM 514 CD1 LEU A 119 209.949 15.963 80.414 1.00 88.09 C ANISOU 514 CD1 LEU A 119 11290 10381 11800 570 218 -12 C ATOM 515 CD2 LEU A 119 208.223 14.479 79.371 1.00 88.48 C ANISOU 515 CD2 LEU A 119 11109 10723 11786 514 359 -73 C ATOM 516 N ALA A 120 212.729 11.828 78.210 1.00 76.51 N ANISOU 516 N ALA A 120 9864 8819 10389 -29 590 475 N ATOM 517 CA ALA A 120 213.815 11.531 77.286 1.00 72.67 C ANISOU 517 CA ALA A 120 9424 8256 9932 -116 592 560 C ATOM 518 C ALA A 120 213.969 10.044 77.002 1.00 68.97 C ANISOU 518 C ALA A 120 8900 7837 9470 -202 673 581 C ATOM 519 O ALA A 120 214.436 9.676 75.918 1.00 69.68 O ANISOU 519 O ALA A 120 8980 7919 9575 -253 676 609 O ATOM 520 CB ALA A 120 215.135 12.082 77.833 1.00 71.40 C ANISOU 520 CB ALA A 120 9346 8002 9782 -143 560 600 C ATOM 521 N MET A 121 213.578 9.181 77.946 1.00 67.77 N ANISOU 521 N MET A 121 8717 7738 9295 -230 721 564 N ATOM 522 CA MET A 121 213.853 7.753 77.783 1.00 65.94 C ANISOU 522 CA MET A 121 8477 7505 9072 -315 751 589 C ATOM 523 C MET A 121 212.981 7.104 76.718 1.00 67.78 C ANISOU 523 C MET A 121 8653 7804 9297 -341 774 581 C ATOM 524 O MET A 121 213.525 6.365 75.877 1.00 66.65 O ANISOU 524 O MET A 121 8508 7628 9187 -374 768 593 O ATOM 525 CB MET A 121 213.717 7.038 79.130 1.00 68.07 C ANISOU 525 CB MET A 121 8771 7791 9302 -375 763 594 C ATOM 526 CG MET A 121 214.253 5.619 79.121 1.00 74.16 C ANISOU 526 CG MET A 121 9589 8497 10090 -455 735 625 C ATOM 527 SD MET A 121 214.146 4.850 80.744 1.00 79.47 S ANISOU 527 SD MET A 121 10338 9163 10695 -565 709 658 S ATOM 528 CE MET A 121 215.633 3.856 80.751 1.00 83.18 C ANISOU 528 CE MET A 121 10907 9457 11242 -562 606 675 C ATOM 529 N PRO A 122 211.655 7.298 76.688 1.00 66.67 N ANISOU 529 N PRO A 122 8452 7772 9109 -323 797 543 N ATOM 530 CA PRO A 122 210.859 6.613 75.651 1.00 63.90 C ANISOU 530 CA PRO A 122 8046 7487 8748 -358 821 538 C ATOM 531 C PRO A 122 211.267 6.984 74.234 1.00 62.68 C ANISOU 531 C PRO A 122 7891 7285 8639 -328 797 555 C ATOM 532 O PRO A 122 211.443 6.096 73.390 1.00 61.76 O ANISOU 532 O PRO A 122 7759 7168 8541 -379 810 567 O ATOM 533 CB PRO A 122 209.421 7.050 75.973 1.00 66.32 C ANISOU 533 CB PRO A 122 8268 7946 8985 -322 841 468 C ATOM 534 CG PRO A 122 209.448 7.401 77.412 1.00 67.58 C ANISOU 534 CG PRO A 122 8433 8144 9100 -319 844 437 C ATOM 535 CD PRO A 122 210.786 8.037 77.624 1.00 67.86 C ANISOU 535 CD PRO A 122 8561 8020 9203 -271 801 480 C ATOM 536 N VAL A 123 211.430 8.280 73.953 1.00 62.82 N ANISOU 536 N VAL A 123 7936 7266 8667 -258 747 553 N ATOM 537 CA VAL A 123 211.792 8.711 72.606 1.00 62.35 C ANISOU 537 CA VAL A 123 7892 7177 8622 -273 710 583 C ATOM 538 C VAL A 123 213.148 8.144 72.207 1.00 61.81 C ANISOU 538 C VAL A 123 7833 7078 8573 -350 725 609 C ATOM 539 O VAL A 123 213.337 7.684 71.074 1.00 61.30 O ANISOU 539 O VAL A 123 7729 7054 8507 -401 736 609 O ATOM 540 CB VAL A 123 211.771 10.248 72.517 1.00 62.73 C ANISOU 540 CB VAL A 123 8013 7161 8663 -209 613 590 C ATOM 541 CG1 VAL A 123 212.288 10.711 71.163 1.00 61.80 C ANISOU 541 CG1 VAL A 123 7938 7012 8530 -281 558 645 C ATOM 542 CG2 VAL A 123 210.367 10.773 72.772 1.00 65.03 C ANISOU 542 CG2 VAL A 123 8270 7502 8938 -95 573 518 C ATOM 543 N GLU A 124 214.112 8.163 73.132 1.00 67.77 N ANISOU 543 N GLU A 124 8626 7782 9341 -353 721 612 N ATOM 544 CA GLU A 124 215.426 7.598 72.844 1.00 70.23 C ANISOU 544 CA GLU A 124 8923 8094 9668 -403 724 599 C ATOM 545 C GLU A 124 215.336 6.103 72.572 1.00 67.21 C ANISOU 545 C GLU A 124 8491 7733 9310 -415 744 558 C ATOM 546 O GLU A 124 216.054 5.574 71.715 1.00 65.33 O ANISOU 546 O GLU A 124 8202 7540 9080 -439 738 512 O ATOM 547 CB GLU A 124 216.380 7.871 74.004 1.00 72.77 C ANISOU 547 CB GLU A 124 9292 8356 9999 -389 707 601 C ATOM 548 CG GLU A 124 217.728 7.203 73.849 1.00 76.87 C ANISOU 548 CG GLU A 124 9777 8896 10533 -415 697 552 C ATOM 549 CD GLU A 124 218.619 7.410 75.050 1.00 80.85 C ANISOU 549 CD GLU A 124 10327 9343 11049 -395 675 549 C ATOM 550 OE1 GLU A 124 218.387 8.378 75.803 1.00 81.51 O ANISOU 550 OE1 GLU A 124 10473 9379 11119 -381 669 596 O ATOM 551 OE2 GLU A 124 219.546 6.598 75.243 1.00 83.32 O ANISOU 551 OE2 GLU A 124 10614 9658 11387 -380 650 488 O ATOM 552 N LEU A 125 214.455 5.405 73.287 1.00 64.38 N ANISOU 552 N LEU A 125 8150 7357 8954 -408 756 564 N ATOM 553 CA LEU A 125 214.292 3.974 73.076 1.00 61.38 C ANISOU 553 CA LEU A 125 7764 6967 8590 -437 741 538 C ATOM 554 C LEU A 125 213.742 3.652 71.690 1.00 60.79 C ANISOU 554 C LEU A 125 7624 6961 8512 -454 762 519 C ATOM 555 O LEU A 125 213.954 2.541 71.194 1.00 61.31 O ANISOU 555 O LEU A 125 7677 7016 8601 -465 731 475 O ATOM 556 CB LEU A 125 213.383 3.392 74.162 1.00 60.55 C ANISOU 556 CB LEU A 125 7708 6847 8451 -480 741 569 C ATOM 557 CG LEU A 125 213.348 1.870 74.311 1.00 60.93 C ANISOU 557 CG LEU A 125 7813 6832 8504 -540 679 564 C ATOM 558 CD1 LEU A 125 214.744 1.323 74.554 1.00 61.12 C ANISOU 558 CD1 LEU A 125 7889 6748 8588 -495 589 521 C ATOM 559 CD2 LEU A 125 212.413 1.463 75.436 1.00 61.38 C ANISOU 559 CD2 LEU A 125 7928 6907 8486 -641 677 614 C ATOM 560 N TYR A 126 213.061 4.597 71.044 1.00 60.68 N ANISOU 560 N TYR A 126 7577 7008 8470 -449 793 543 N ATOM 561 CA TYR A 126 212.483 4.351 69.729 1.00 64.43 C ANISOU 561 CA TYR A 126 7994 7552 8935 -472 810 532 C ATOM 562 C TYR A 126 213.320 4.918 68.586 1.00 65.56 C ANISOU 562 C TYR A 126 8101 7744 9067 -500 800 521 C ATOM 563 O TYR A 126 213.635 4.195 67.637 1.00 64.74 O ANISOU 563 O TYR A 126 7936 7698 8965 -529 804 472 O ATOM 564 CB TYR A 126 211.063 4.923 69.651 1.00 68.43 C ANISOU 564 CB TYR A 126 8484 8109 9407 -454 829 555 C ATOM 565 CG TYR A 126 210.520 4.911 68.242 1.00 68.37 C ANISOU 565 CG TYR A 126 8423 8167 9386 -473 837 552 C ATOM 566 CD1 TYR A 126 210.142 3.722 67.635 1.00 66.68 C ANISOU 566 CD1 TYR A 126 8167 7992 9176 -514 860 528 C ATOM 567 CD2 TYR A 126 210.414 6.086 67.510 1.00 68.80 C ANISOU 567 CD2 TYR A 126 8488 8231 9420 -461 801 577 C ATOM 568 CE1 TYR A 126 209.660 3.705 66.342 1.00 66.48 C ANISOU 568 CE1 TYR A 126 8090 8034 9136 -536 870 523 C ATOM 569 CE2 TYR A 126 209.934 6.079 66.217 1.00 68.35 C ANISOU 569 CE2 TYR A 126 8393 8233 9343 -493 797 582 C ATOM 570 CZ TYR A 126 209.557 4.886 65.638 1.00 68.39 C ANISOU 570 CZ TYR A 126 8335 8296 9354 -527 843 552 C ATOM 571 OH TYR A 126 209.078 4.878 64.349 1.00 70.79 O ANISOU 571 OH TYR A 126 8596 8666 9635 -562 842 555 O ATOM 572 N ASN A 127 213.672 6.201 68.646 1.00 69.05 N ANISOU 572 N ASN A 127 8582 8172 9480 -508 776 562 N ATOM 573 CA ASN A 127 214.327 6.873 67.531 1.00 72.08 C ANISOU 573 CA ASN A 127 8951 8622 9815 -590 754 574 C ATOM 574 C ASN A 127 215.844 6.908 67.643 1.00 70.91 C ANISOU 574 C ASN A 127 8779 8517 9646 -642 748 535 C ATOM 575 O ASN A 127 216.506 7.372 66.709 1.00 72.59 O ANISOU 575 O ASN A 127 8960 8834 9788 -751 737 534 O ATOM 576 CB ASN A 127 213.793 8.301 67.383 1.00 73.65 C ANISOU 576 CB ASN A 127 9236 8772 9977 -598 691 649 C ATOM 577 CG ASN A 127 212.679 8.399 66.364 1.00 75.02 C ANISOU 577 CG ASN A 127 9395 8976 10131 -602 674 667 C ATOM 578 OD1 ASN A 127 211.661 9.045 66.598 1.00 76.68 O ANISOU 578 OD1 ASN A 127 9654 9133 10349 -525 624 684 O ATOM 579 ND2 ASN A 127 212.868 7.750 65.222 1.00 75.26 N ANISOU 579 ND2 ASN A 127 9351 9108 10137 -680 707 645 N ATOM 580 N PHE A 128 216.413 6.433 68.749 1.00 65.19 N ANISOU 580 N PHE A 128 8066 7737 8967 -582 750 499 N ATOM 581 CA PHE A 128 217.858 6.392 68.905 1.00 62.69 C ANISOU 581 CA PHE A 128 7708 7480 8633 -611 738 436 C ATOM 582 C PHE A 128 218.402 5.002 69.191 1.00 63.95 C ANISOU 582 C PHE A 128 7807 7642 8849 -536 725 320 C ATOM 583 O PHE A 128 219.622 4.815 69.126 1.00 66.17 O ANISOU 583 O PHE A 128 8016 8011 9114 -540 705 222 O ATOM 584 CB PHE A 128 218.307 7.340 70.028 1.00 61.46 C ANISOU 584 CB PHE A 128 7640 7241 8472 -604 715 491 C ATOM 585 CG PHE A 128 217.970 8.778 69.775 1.00 60.71 C ANISOU 585 CG PHE A 128 7632 7117 8320 -671 680 589 C ATOM 586 CD1 PHE A 128 218.028 9.302 68.496 1.00 61.42 C ANISOU 586 CD1 PHE A 128 7709 7299 8329 -795 659 618 C ATOM 587 CD2 PHE A 128 217.598 9.609 70.817 1.00 59.69 C ANISOU 587 CD2 PHE A 128 7607 6862 8209 -614 645 647 C ATOM 588 CE1 PHE A 128 217.719 10.626 68.258 1.00 61.46 C ANISOU 588 CE1 PHE A 128 7834 7239 8278 -863 580 716 C ATOM 589 CE2 PHE A 128 217.288 10.934 70.586 1.00 59.88 C ANISOU 589 CE2 PHE A 128 7735 6827 8188 -653 568 722 C ATOM 590 CZ PHE A 128 217.349 11.444 69.305 1.00 60.78 C ANISOU 590 CZ PHE A 128 7866 7002 8227 -780 524 763 C ATOM 591 N ILE A 129 217.547 4.027 69.499 1.00 63.54 N ANISOU 591 N ILE A 129 7787 7502 8855 -473 716 320 N ATOM 592 CA ILE A 129 217.970 2.671 69.823 1.00 65.83 C ANISOU 592 CA ILE A 129 8069 7741 9201 -402 653 221 C ATOM 593 C ILE A 129 217.444 1.662 68.809 1.00 67.60 C ANISOU 593 C ILE A 129 8242 8002 9440 -394 640 159 C ATOM 594 O ILE A 129 218.195 0.821 68.304 1.00 71.16 O ANISOU 594 O ILE A 129 8620 8504 9912 -343 581 18 O ATOM 595 CB ILE A 129 217.546 2.275 71.255 1.00 65.08 C ANISOU 595 CB ILE A 129 8098 7485 9146 -367 615 282 C ATOM 596 CG1 ILE A 129 218.170 3.218 72.284 1.00 63.94 C ANISOU 596 CG1 ILE A 129 7996 7308 8990 -364 623 326 C ATOM 597 CG2 ILE A 129 217.942 0.836 71.547 1.00 68.10 C ANISOU 597 CG2 ILE A 129 8517 7776 9583 -306 503 194 C ATOM 598 CD1 ILE A 129 219.674 3.115 72.367 1.00 66.23 C ANISOU 598 CD1 ILE A 129 8234 7640 9291 -325 574 220 C ATOM 599 N TRP A 130 216.151 1.730 68.497 1.00 66.08 N ANISOU 599 N TRP A 130 8078 7795 9235 -434 684 245 N ATOM 600 CA TRP A 130 215.513 0.725 67.654 1.00 67.39 C ANISOU 600 CA TRP A 130 8214 7977 9414 -435 669 202 C ATOM 601 C TRP A 130 215.351 1.172 66.205 1.00 68.31 C ANISOU 601 C TRP A 130 8226 8247 9483 -489 727 184 C ATOM 602 O TRP A 130 215.742 0.444 65.288 1.00 71.49 O ANISOU 602 O TRP A 130 8543 8734 9888 -476 703 70 O ATOM 603 CB TRP A 130 214.153 0.339 68.248 1.00 64.31 C ANISOU 603 CB TRP A 130 7914 7497 9023 -465 676 297 C ATOM 604 CG TRP A 130 214.265 -0.669 69.351 1.00 64.24 C ANISOU 604 CG TRP A 130 8016 7346 9047 -452 582 293 C ATOM 605 CD1 TRP A 130 214.345 -0.417 70.690 1.00 63.17 C ANISOU 605 CD1 TRP A 130 7967 7129 8904 -463 566 355 C ATOM 606 CD2 TRP A 130 214.312 -2.093 69.207 1.00 65.83 C ANISOU 606 CD2 TRP A 130 8274 7457 9283 -437 467 228 C ATOM 607 NE1 TRP A 130 214.440 -1.597 71.389 1.00 63.70 N ANISOU 607 NE1 TRP A 130 8151 7062 8992 -475 445 345 N ATOM 608 CE2 TRP A 130 214.421 -2.641 70.502 1.00 65.11 C ANISOU 608 CE2 TRP A 130 8323 7216 9199 -455 369 269 C ATOM 609 CE3 TRP A 130 214.275 -2.959 68.110 1.00 67.93 C ANISOU 609 CE3 TRP A 130 8494 7745 9570 -413 418 136 C ATOM 610 CZ2 TRP A 130 214.492 -4.014 70.728 1.00 66.17 C ANISOU 610 CZ2 TRP A 130 8581 7199 9361 -457 202 232 C ATOM 611 CZ3 TRP A 130 214.345 -4.321 68.337 1.00 68.86 C ANISOU 611 CZ3 TRP A 130 8722 7715 9726 -393 258 83 C ATOM 612 CH2 TRP A 130 214.453 -4.835 69.636 1.00 67.88 C ANISOU 612 CH2 TRP A 130 8763 7418 9608 -418 140 136 C ATOM 613 N VAL A 131 214.784 2.349 65.975 1.00 65.76 N ANISOU 613 N VAL A 131 7915 7960 9112 -547 783 286 N ATOM 614 CA VAL A 131 214.554 2.864 64.626 1.00 64.98 C ANISOU 614 CA VAL A 131 7748 7989 8954 -622 816 296 C ATOM 615 C VAL A 131 215.309 4.184 64.528 1.00 65.89 C ANISOU 615 C VAL A 131 7871 8161 9002 -698 815 340 C ATOM 616 O VAL A 131 214.789 5.248 64.877 1.00 65.01 O ANISOU 616 O VAL A 131 7847 7981 8873 -712 804 445 O ATOM 617 CB VAL A 131 213.068 3.040 64.313 1.00 64.26 C ANISOU 617 CB VAL A 131 7688 7871 8856 -631 840 378 C ATOM 618 CG1 VAL A 131 212.887 3.544 62.892 1.00 67.77 C ANISOU 618 CG1 VAL A 131 8078 8436 9238 -715 853 392 C ATOM 619 CG2 VAL A 131 212.327 1.726 64.517 1.00 64.53 C ANISOU 619 CG2 VAL A 131 7729 7855 8935 -593 836 347 C ATOM 620 N HIS A 132 216.549 4.121 64.033 1.00 67.12 N ANISOU 620 N HIS A 132 7936 8457 9110 -752 811 246 N ATOM 621 CA HIS A 132 217.415 5.297 64.037 1.00 65.64 C ANISOU 621 CA HIS A 132 7763 8339 8838 -861 802 286 C ATOM 622 C HIS A 132 216.919 6.375 63.081 1.00 64.99 C ANISOU 622 C HIS A 132 7728 8304 8662 -1003 789 397 C ATOM 623 O HIS A 132 217.199 7.559 63.292 1.00 65.16 O ANISOU 623 O HIS A 132 7842 8292 8622 -1092 745 490 O ATOM 624 CB HIS A 132 218.846 4.891 63.690 1.00 66.90 C ANISOU 624 CB HIS A 132 7780 8695 8944 -902 804 131 C ATOM 625 CG HIS A 132 219.470 3.968 64.690 1.00 68.23 C ANISOU 625 CG HIS A 132 7926 8795 9203 -752 774 16 C ATOM 626 ND1 HIS A 132 218.969 2.713 64.960 1.00 69.35 N ANISOU 626 ND1 HIS A 132 8079 8824 9448 -614 742 -47 N ATOM 627 CD2 HIS A 132 220.549 4.122 65.494 1.00 70.06 C ANISOU 627 CD2 HIS A 132 8144 9042 9433 -725 750 -42 C ATOM 628 CE1 HIS A 132 219.715 2.130 65.881 1.00 71.35 C ANISOU 628 CE1 HIS A 132 8339 9010 9760 -507 683 -136 C ATOM 629 NE2 HIS A 132 220.680 2.964 66.223 1.00 72.88 N ANISOU 629 NE2 HIS A 132 8508 9287 9898 -561 694 -141 N ATOM 630 N HIS A 133 216.190 5.994 62.039 1.00 64.84 N ANISOU 630 N HIS A 133 7663 8346 8628 -1031 805 392 N ATOM 631 CA HIS A 133 215.626 6.959 61.103 1.00 64.73 C ANISOU 631 CA HIS A 133 7712 8354 8527 -1162 767 502 C ATOM 632 C HIS A 133 214.374 6.384 60.448 1.00 64.48 C ANISOU 632 C HIS A 133 7661 8301 8536 -1106 785 509 C ATOM 633 O HIS A 133 214.286 5.172 60.244 1.00 64.45 O ANISOU 633 O HIS A 133 7555 8350 8583 -1038 835 406 O ATOM 634 CB HIS A 133 216.659 7.351 60.041 1.00 66.66 C ANISOU 634 CB HIS A 133 7882 8829 8618 -1382 762 475 C ATOM 635 CG HIS A 133 217.022 6.238 59.107 1.00 73.98 C ANISOU 635 CG HIS A 133 8619 9973 9516 -1403 825 320 C ATOM 636 ND1 HIS A 133 216.239 5.883 58.029 1.00 78.71 N ANISOU 636 ND1 HIS A 133 9178 10633 10096 -1438 839 322 N ATOM 637 CD2 HIS A 133 218.093 5.408 59.082 1.00 75.96 C ANISOU 637 CD2 HIS A 133 8704 10403 9756 -1379 862 136 C ATOM 638 CE1 HIS A 133 216.807 4.879 57.386 1.00 78.35 C ANISOU 638 CE1 HIS A 133 8951 10791 10028 -1438 886 148 C ATOM 639 NE2 HIS A 133 217.934 4.573 58.004 1.00 76.70 N ANISOU 639 NE2 HIS A 133 8660 10659 9825 -1393 893 22 N ATOM 640 N PRO A 134 213.402 7.249 60.104 1.00 64.08 N ANISOU 640 N PRO A 134 7715 8167 8464 -1128 724 621 N ATOM 641 CA PRO A 134 213.429 8.710 60.250 1.00 64.04 C ANISOU 641 CA PRO A 134 7865 8065 8400 -1201 616 739 C ATOM 642 C PRO A 134 212.930 9.219 61.603 1.00 64.18 C ANISOU 642 C PRO A 134 7988 7893 8505 -1040 574 771 C ATOM 643 O PRO A 134 212.336 8.463 62.370 1.00 67.82 O ANISOU 643 O PRO A 134 8402 8308 9059 -889 634 717 O ATOM 644 CB PRO A 134 212.495 9.175 59.134 1.00 64.12 C ANISOU 644 CB PRO A 134 7929 8073 8359 -1266 544 811 C ATOM 645 CG PRO A 134 211.482 8.091 59.052 1.00 64.10 C ANISOU 645 CG PRO A 134 7830 8081 8445 -1127 623 744 C ATOM 646 CD PRO A 134 212.198 6.802 59.379 1.00 63.79 C ANISOU 646 CD PRO A 134 7652 8134 8450 -1089 736 626 C ATOM 647 N TRP A 135 213.175 10.499 61.879 1.00 63.83 N ANISOU 647 N TRP A 135 8090 7746 8415 -1090 458 855 N ATOM 648 CA TRP A 135 212.679 11.129 63.098 1.00 63.92 C ANISOU 648 CA TRP A 135 8202 7588 8498 -933 396 869 C ATOM 649 C TRP A 135 211.173 11.339 62.990 1.00 64.46 C ANISOU 649 C TRP A 135 8299 7579 8613 -792 334 863 C ATOM 650 O TRP A 135 210.697 12.013 62.069 1.00 65.18 O ANISOU 650 O TRP A 135 8474 7637 8654 -846 216 919 O ATOM 651 CB TRP A 135 213.398 12.456 63.328 1.00 67.68 C ANISOU 651 CB TRP A 135 8840 7968 8907 -1032 262 952 C ATOM 652 CG TRP A 135 212.884 13.238 64.498 1.00 70.74 C ANISOU 652 CG TRP A 135 9340 8178 9362 -863 170 951 C ATOM 653 CD1 TRP A 135 212.096 14.352 64.458 1.00 71.06 C ANISOU 653 CD1 TRP A 135 9534 8062 9401 -790 -16 987 C ATOM 654 CD2 TRP A 135 213.129 12.968 65.883 1.00 68.97 C ANISOU 654 CD2 TRP A 135 9078 7920 9208 -739 241 895 C ATOM 655 NE1 TRP A 135 211.834 14.792 65.733 1.00 69.22 N ANISOU 655 NE1 TRP A 135 9344 7720 9236 -617 -56 938 N ATOM 656 CE2 TRP A 135 212.456 13.959 66.626 1.00 69.42 C ANISOU 656 CE2 TRP A 135 9253 7825 9300 -598 110 890 C ATOM 657 CE3 TRP A 135 213.850 11.985 66.567 1.00 65.66 C ANISOU 657 CE3 TRP A 135 8542 7580 8824 -730 384 839 C ATOM 658 CZ2 TRP A 135 212.482 13.993 68.018 1.00 69.75 C ANISOU 658 CZ2 TRP A 135 9284 7819 9399 -468 141 835 C ATOM 659 CZ3 TRP A 135 213.876 12.021 67.948 1.00 65.15 C ANISOU 659 CZ3 TRP A 135 8491 7445 8818 -610 404 805 C ATOM 660 CH2 TRP A 135 213.197 13.019 68.659 1.00 67.23 C ANISOU 660 CH2 TRP A 135 8857 7583 9104 -490 295 805 C ATOM 661 N ALA A 136 210.421 10.772 63.933 1.00 64.52 N ANISOU 661 N ALA A 136 8237 7574 8701 -624 402 790 N ATOM 662 CA ALA A 136 208.970 10.691 63.828 1.00 66.03 C ANISOU 662 CA ALA A 136 8395 7771 8924 -495 380 745 C ATOM 663 C ALA A 136 208.247 11.725 64.682 1.00 67.66 C ANISOU 663 C ALA A 136 8679 7871 9156 -333 256 709 C ATOM 664 O ALA A 136 207.087 11.511 65.046 1.00 69.33 O ANISOU 664 O ALA A 136 8814 8135 9394 -196 269 623 O ATOM 665 CB ALA A 136 208.496 9.285 64.197 1.00 65.60 C ANISOU 665 CB ALA A 136 8194 7821 8910 -453 533 675 C ATOM 666 N PHE A 137 208.893 12.847 64.999 1.00 67.36 N ANISOU 666 N PHE A 137 8788 7704 9101 -347 125 757 N ATOM 667 CA PHE A 137 208.282 13.852 65.858 1.00 68.59 C ANISOU 667 CA PHE A 137 9023 7750 9287 -170 -16 697 C ATOM 668 C PHE A 137 208.389 15.267 65.299 1.00 68.33 C ANISOU 668 C PHE A 137 9203 7541 9218 -189 -269 763 C ATOM 669 O PHE A 137 208.019 16.222 65.992 1.00 68.76 O ANISOU 669 O PHE A 137 9354 7472 9300 -33 -431 704 O ATOM 670 CB PHE A 137 208.893 13.789 67.265 1.00 70.80 C ANISOU 670 CB PHE A 137 9286 8019 9597 -127 56 664 C ATOM 671 CG PHE A 137 208.775 12.435 67.916 1.00 70.84 C ANISOU 671 CG PHE A 137 9123 8167 9626 -123 262 610 C ATOM 672 CD1 PHE A 137 207.553 11.985 68.392 1.00 69.56 C ANISOU 672 CD1 PHE A 137 8843 8112 9475 -3 311 504 C ATOM 673 CD2 PHE A 137 209.878 11.611 68.048 1.00 70.83 C ANISOU 673 CD2 PHE A 137 9088 8200 9625 -248 384 656 C ATOM 674 CE1 PHE A 137 207.435 10.744 68.987 1.00 69.22 C ANISOU 674 CE1 PHE A 137 8680 8188 9432 -42 472 475 C ATOM 675 CE2 PHE A 137 209.763 10.367 68.644 1.00 66.11 C ANISOU 675 CE2 PHE A 137 8378 7694 9048 -248 526 614 C ATOM 676 CZ PHE A 137 208.540 9.935 69.113 1.00 66.42 C ANISOU 676 CZ PHE A 137 8329 7819 9088 -163 566 538 C ATOM 677 N GLY A 138 208.878 15.431 64.072 1.00 67.54 N ANISOU 677 N GLY A 138 9189 7426 9048 -385 -326 878 N ATOM 678 CA GLY A 138 208.880 16.729 63.428 1.00 67.72 C ANISOU 678 CA GLY A 138 9446 7270 9017 -441 -599 961 C ATOM 679 C GLY A 138 209.954 17.665 63.949 1.00 66.96 C ANISOU 679 C GLY A 138 9530 7034 8876 -545 -718 1041 C ATOM 680 O GLY A 138 210.713 17.362 64.872 1.00 66.14 O ANISOU 680 O GLY A 138 9361 6977 8793 -554 -583 1023 O ATOM 681 N ASP A 139 210.006 18.846 63.326 1.00 67.45 N ANISOU 681 N ASP A 139 9844 6912 8870 -638 -998 1138 N ATOM 682 CA ASP A 139 211.015 19.838 63.689 1.00 72.33 C ANISOU 682 CA ASP A 139 10676 7383 9423 -781 -1151 1236 C ATOM 683 C ASP A 139 210.772 20.390 65.088 1.00 76.59 C ANISOU 683 C ASP A 139 11254 7788 10059 -526 -1228 1127 C ATOM 684 O ASP A 139 211.722 20.600 65.853 1.00 74.70 O ANISOU 684 O ASP A 139 11051 7529 9803 -600 -1186 1158 O ATOM 685 CB ASP A 139 211.032 20.968 62.659 1.00 77.54 C ANISOU 685 CB ASP A 139 11633 7855 9974 -962 -1473 1377 C ATOM 686 CG ASP A 139 212.135 21.981 62.917 1.00 81.13 C ANISOU 686 CG ASP A 139 12333 8167 10327 -1179 -1645 1504 C ATOM 687 OD1 ASP A 139 213.312 21.671 62.634 1.00 81.66 O ANISOU 687 OD1 ASP A 139 12352 8399 10277 -1479 -1500 1599 O ATOM 688 OD2 ASP A 139 211.825 23.090 63.401 1.00 83.69 O ANISOU 688 OD2 ASP A 139 12892 8222 10682 -1048 -1937 1496 O ATOM 689 N ALA A 140 209.507 20.636 65.440 1.00 79.45 N ANISOU 689 N ALA A 140 11595 8079 10513 -225 -1342 982 N ATOM 690 CA ALA A 140 209.194 21.116 66.782 1.00 76.79 C ANISOU 690 CA ALA A 140 11257 7661 10258 33 -1407 840 C ATOM 691 C ALA A 140 209.548 20.072 67.835 1.00 76.71 C ANISOU 691 C ALA A 140 11000 7855 10292 65 -1084 771 C ATOM 692 O ALA A 140 210.044 20.411 68.917 1.00 79.00 O ANISOU 692 O ALA A 140 11318 8095 10603 118 -1082 739 O ATOM 693 CB ALA A 140 207.717 21.499 66.873 1.00 73.58 C ANISOU 693 CB ALA A 140 10827 7207 9925 354 -1584 657 C ATOM 694 N GLY A 141 209.305 18.795 67.535 1.00 72.15 N ANISOU 694 N GLY A 141 10196 7494 9723 27 -827 751 N ATOM 695 CA GLY A 141 209.724 17.742 68.441 1.00 70.74 C ANISOU 695 CA GLY A 141 9823 7482 9573 19 -553 710 C ATOM 696 C GLY A 141 211.229 17.585 68.509 1.00 70.54 C ANISOU 696 C GLY A 141 9840 7462 9499 -207 -461 832 C ATOM 697 O GLY A 141 211.774 17.248 69.565 1.00 74.26 O ANISOU 697 O GLY A 141 10244 7975 9997 -184 -339 801 O ATOM 698 N CYS A 142 211.922 17.826 67.395 1.00 68.72 N ANISOU 698 N CYS A 142 9714 7212 9184 -437 -521 963 N ATOM 699 CA CYS A 142 213.379 17.740 67.398 1.00 68.83 C ANISOU 699 CA CYS A 142 9747 7278 9126 -666 -444 1054 C ATOM 700 C CYS A 142 213.986 18.833 68.269 1.00 65.93 C ANISOU 700 C CYS A 142 9556 6748 8747 -665 -591 1085 C ATOM 701 O CYS A 142 214.882 18.570 69.078 1.00 63.84 O ANISOU 701 O CYS A 142 9235 6536 8485 -704 -473 1079 O ATOM 702 CB CYS A 142 213.909 17.821 65.965 1.00 75.02 C ANISOU 702 CB CYS A 142 10589 8125 9789 -939 -486 1171 C ATOM 703 SG CYS A 142 215.703 17.610 65.793 1.00 79.25 S ANISOU 703 SG CYS A 142 11086 8823 10200 -1249 -372 1243 S ATOM 704 N ARG A 143 213.499 20.069 68.123 1.00 72.77 N ANISOU 704 N ARG A 143 10647 7401 9601 -610 -870 1111 N ATOM 705 CA ARG A 143 213.994 21.165 68.949 1.00 77.27 C ANISOU 705 CA ARG A 143 11409 7788 10163 -594 -1045 1132 C ATOM 706 C ARG A 143 213.553 21.018 70.399 1.00 77.31 C ANISOU 706 C ARG A 143 11304 7792 10279 -318 -970 980 C ATOM 707 O ARG A 143 214.301 21.382 71.314 1.00 78.68 O ANISOU 707 O ARG A 143 11529 7914 10451 -334 -971 987 O ATOM 708 CB ARG A 143 213.515 22.506 68.391 1.00 79.69 C ANISOU 708 CB ARG A 143 12010 7836 10432 -588 -1411 1186 C ATOM 709 CG ARG A 143 213.919 22.782 66.953 1.00 80.81 C ANISOU 709 CG ARG A 143 12301 7967 10435 -902 -1527 1356 C ATOM 710 CD ARG A 143 213.389 24.134 66.498 1.00 83.21 C ANISOU 710 CD ARG A 143 12940 7969 10708 -883 -1939 1412 C ATOM 711 NE ARG A 143 213.554 24.337 65.063 1.00 88.26 N ANISOU 711 NE ARG A 143 13722 8605 11207 -1183 -2063 1573 N ATOM 712 CZ ARG A 143 214.654 24.822 64.497 1.00 93.80 C ANISOU 712 CZ ARG A 143 14599 9308 11732 -1574 -2147 1755 C ATOM 713 NH1 ARG A 143 215.695 25.157 65.247 1.00 96.14 N ANISOU 713 NH1 ARG A 143 14949 9602 11980 -1700 -2120 1797 N ATOM 714 NH2 ARG A 143 214.713 24.970 63.181 1.00 96.47 N ANISOU 714 NH2 ARG A 143 15055 9674 11927 -1860 -2257 1894 N ATOM 715 N GLY A 144 212.352 20.495 70.629 1.00 76.19 N ANISOU 715 N GLY A 144 11005 7728 10217 -85 -905 839 N ATOM 716 CA GLY A 144 211.824 20.357 71.972 1.00 75.14 C ANISOU 716 CA GLY A 144 10750 7640 10160 151 -838 681 C ATOM 717 C GLY A 144 212.465 19.244 72.775 1.00 75.60 C ANISOU 717 C GLY A 144 10622 7872 10230 90 -553 677 C ATOM 718 O GLY A 144 212.719 19.404 73.972 1.00 76.93 O ANISOU 718 O GLY A 144 10774 8032 10423 171 -524 618 O ATOM 719 N TYR A 145 212.725 18.106 72.128 1.00 72.15 N ANISOU 719 N TYR A 145 10053 7586 9776 -48 -361 731 N ATOM 720 CA TYR A 145 213.311 16.968 72.832 1.00 68.12 C ANISOU 720 CA TYR A 145 9385 7216 9282 -95 -129 720 C ATOM 721 C TYR A 145 214.700 17.302 73.358 1.00 71.42 C ANISOU 721 C TYR A 145 9883 7582 9672 -219 -124 791 C ATOM 722 O TYR A 145 214.997 17.098 74.541 1.00 77.38 O ANISOU 722 O TYR A 145 10592 8354 10455 -158 -49 746 O ATOM 723 CB TYR A 145 213.369 15.752 71.909 1.00 63.56 C ANISOU 723 CB TYR A 145 8678 6781 8693 -209 26 752 C ATOM 724 CG TYR A 145 214.075 14.562 72.512 1.00 62.02 C ANISOU 724 CG TYR A 145 8355 6696 8515 -261 215 741 C ATOM 725 CD1 TYR A 145 213.392 13.666 73.317 1.00 62.23 C ANISOU 725 CD1 TYR A 145 8261 6805 8580 -163 326 663 C ATOM 726 CD2 TYR A 145 215.423 14.333 72.275 1.00 60.93 C ANISOU 726 CD2 TYR A 145 8222 6588 8342 -417 261 800 C ATOM 727 CE1 TYR A 145 214.028 12.576 73.871 1.00 61.03 C ANISOU 727 CE1 TYR A 145 8031 6716 8442 -215 454 661 C ATOM 728 CE2 TYR A 145 216.070 13.246 72.828 1.00 60.05 C ANISOU 728 CE2 TYR A 145 8004 6556 8254 -434 395 769 C ATOM 729 CZ TYR A 145 215.366 12.370 73.624 1.00 59.88 C ANISOU 729 CZ TYR A 145 7899 6569 8282 -330 478 708 C ATOM 730 OH TYR A 145 215.997 11.281 74.179 1.00 58.93 O ANISOU 730 OH TYR A 145 7713 6494 8186 -352 569 685 O ATOM 731 N TYR A 146 215.573 17.812 72.487 1.00 70.98 N ANISOU 731 N TYR A 146 9944 7483 9542 -413 -204 902 N ATOM 732 CA TYR A 146 216.932 18.129 72.906 1.00 74.75 C ANISOU 732 CA TYR A 146 10482 7948 9970 -559 -197 963 C ATOM 733 C TYR A 146 216.986 19.317 73.857 1.00 73.10 C ANISOU 733 C TYR A 146 10437 7564 9772 -474 -359 957 C ATOM 734 O TYR A 146 217.960 19.449 74.606 1.00 76.71 O ANISOU 734 O TYR A 146 10912 8021 10213 -537 -322 976 O ATOM 735 CB TYR A 146 217.811 18.379 71.679 1.00 79.59 C ANISOU 735 CB TYR A 146 11161 8613 10466 -829 -242 1074 C ATOM 736 CG TYR A 146 218.318 17.107 71.037 1.00 82.87 C ANISOU 736 CG TYR A 146 11379 9248 10859 -933 -49 1051 C ATOM 737 CD1 TYR A 146 219.523 16.538 71.433 1.00 80.78 C ANISOU 737 CD1 TYR A 146 11009 9112 10570 -1019 74 1026 C ATOM 738 CD2 TYR A 146 217.584 16.462 70.050 1.00 85.58 C ANISOU 738 CD2 TYR A 146 11637 9670 11211 -925 -4 1036 C ATOM 739 CE1 TYR A 146 219.988 15.370 70.855 1.00 80.91 C ANISOU 739 CE1 TYR A 146 10843 9326 10574 -1079 218 970 C ATOM 740 CE2 TYR A 146 218.041 15.293 69.467 1.00 85.18 C ANISOU 740 CE2 TYR A 146 11409 9813 11145 -1001 152 994 C ATOM 741 CZ TYR A 146 219.243 14.751 69.873 1.00 82.77 C ANISOU 741 CZ TYR A 146 11002 9627 10819 -1069 255 953 C ATOM 742 OH TYR A 146 219.700 13.589 69.294 1.00 83.80 O ANISOU 742 OH TYR A 146 10955 9946 10940 -1112 378 877 O ATOM 743 N PHE A 147 215.968 20.177 73.857 1.00 70.15 N ANISOU 743 N PHE A 147 10180 7044 9428 -319 -550 913 N ATOM 744 CA PHE A 147 215.922 21.251 74.843 1.00 70.02 C ANISOU 744 CA PHE A 147 10307 6862 9437 -193 -717 867 C ATOM 745 C PHE A 147 215.600 20.706 76.227 1.00 71.10 C ANISOU 745 C PHE A 147 10280 7090 9644 -7 -569 736 C ATOM 746 O PHE A 147 216.296 21.008 77.204 1.00 76.56 O ANISOU 746 O PHE A 147 11008 7744 10336 -11 -560 734 O ATOM 747 CB PHE A 147 214.895 22.305 74.435 1.00 69.14 C ANISOU 747 CB PHE A 147 10362 6568 9341 -46 -998 821 C ATOM 748 CG PHE A 147 214.660 23.356 75.483 1.00 65.87 C ANISOU 748 CG PHE A 147 10074 5987 8967 146 -1192 723 C ATOM 749 CD1 PHE A 147 215.548 24.405 75.642 1.00 65.93 C ANISOU 749 CD1 PHE A 147 10324 5804 8924 24 -1382 818 C ATOM 750 CD2 PHE A 147 213.549 23.298 76.307 1.00 65.08 C ANISOU 750 CD2 PHE A 147 9843 5942 8941 439 -1190 521 C ATOM 751 CE1 PHE A 147 215.333 25.375 76.604 1.00 63.45 C ANISOU 751 CE1 PHE A 147 10133 5324 8650 213 -1578 715 C ATOM 752 CE2 PHE A 147 213.330 24.265 77.270 1.00 65.41 C ANISOU 752 CE2 PHE A 147 9982 5855 9017 633 -1375 397 C ATOM 753 CZ PHE A 147 214.224 25.304 77.418 1.00 64.51 C ANISOU 753 CZ PHE A 147 10123 5519 8870 531 -1575 494 C ATOM 754 N LEU A 148 214.544 19.898 76.329 1.00 67.05 N ANISOU 754 N LEU A 148 9589 6711 9176 134 -454 630 N ATOM 755 CA LEU A 148 214.138 19.374 77.627 1.00 65.92 C ANISOU 755 CA LEU A 148 9294 6684 9069 272 -324 507 C ATOM 756 C LEU A 148 215.153 18.376 78.166 1.00 69.59 C ANISOU 756 C LEU A 148 9667 7248 9526 136 -118 570 C ATOM 757 O LEU A 148 215.417 18.344 79.373 1.00 74.32 O ANISOU 757 O LEU A 148 10236 7868 10135 182 -67 525 O ATOM 758 CB LEU A 148 212.759 18.730 77.520 1.00 66.90 C ANISOU 758 CB LEU A 148 9250 6957 9210 406 -258 385 C ATOM 759 CG LEU A 148 211.635 19.668 77.082 1.00 67.86 C ANISOU 759 CG LEU A 148 9432 7006 9346 591 -474 275 C ATOM 760 CD1 LEU A 148 210.326 18.906 76.955 1.00 69.67 C ANISOU 760 CD1 LEU A 148 9460 7437 9576 697 -378 148 C ATOM 761 CD2 LEU A 148 211.497 20.837 78.043 1.00 69.27 C ANISOU 761 CD2 LEU A 148 9704 7075 9542 769 -658 155 C ATOM 762 N ARG A 149 215.734 17.552 77.290 1.00 71.05 N ANISOU 762 N ARG A 149 9805 7497 9692 -23 -13 661 N ATOM 763 CA ARG A 149 216.691 16.555 77.754 1.00 74.02 C ANISOU 763 CA ARG A 149 10094 7961 10069 -123 148 692 C ATOM 764 C ARG A 149 217.936 17.205 78.341 1.00 79.12 C ANISOU 764 C ARG A 149 10839 8531 10692 -200 105 743 C ATOM 765 O ARG A 149 218.527 16.672 79.288 1.00 82.81 O ANISOU 765 O ARG A 149 11251 9040 11173 -203 199 728 O ATOM 766 CB ARG A 149 217.074 15.613 76.612 1.00 76.88 C ANISOU 766 CB ARG A 149 10381 8414 10415 -252 237 743 C ATOM 767 CG ARG A 149 217.956 14.453 77.049 1.00 79.83 C ANISOU 767 CG ARG A 149 10656 8874 10801 -312 372 739 C ATOM 768 CD ARG A 149 218.529 13.713 75.856 1.00 84.15 C ANISOU 768 CD ARG A 149 11135 9515 11325 -432 424 761 C ATOM 769 NE ARG A 149 219.470 12.671 76.258 1.00 87.34 N ANISOU 769 NE ARG A 149 11454 9986 11745 -460 508 728 N ATOM 770 CZ ARG A 149 219.153 11.389 76.396 1.00 88.80 C ANISOU 770 CZ ARG A 149 11553 10215 11972 -415 578 683 C ATOM 771 NH1 ARG A 149 217.913 10.982 76.160 1.00 89.83 N ANISOU 771 NH1 ARG A 149 11655 10356 12121 -363 599 673 N ATOM 772 NH2 ARG A 149 220.077 10.512 76.765 1.00 89.84 N ANISOU 772 NH2 ARG A 149 11635 10378 12123 -425 608 643 N ATOM 773 N ASP A 150 218.348 18.353 77.805 1.00 83.10 N ANISOU 773 N ASP A 150 11502 8922 11152 -277 -50 808 N ATOM 774 CA ASP A 150 219.503 19.042 78.367 1.00 89.19 C ANISOU 774 CA ASP A 150 12377 9626 11884 -370 -102 858 C ATOM 775 C ASP A 150 219.116 19.892 79.570 1.00 87.72 C ANISOU 775 C ASP A 150 12274 9323 11733 -212 -201 793 C ATOM 776 O ASP A 150 219.885 19.995 80.532 1.00 87.88 O ANISOU 776 O ASP A 150 12304 9335 11751 -229 -167 794 O ATOM 777 CB ASP A 150 220.179 19.898 77.296 1.00 97.49 C ANISOU 777 CB ASP A 150 13581 10619 12843 -573 -238 969 C ATOM 778 CG ASP A 150 220.811 19.063 76.197 1.00100.97 C ANISOU 778 CG ASP A 150 13911 11230 13225 -756 -125 1012 C ATOM 779 OD1 ASP A 150 220.457 17.870 76.078 1.00101.49 O ANISOU 779 OD1 ASP A 150 13806 11415 13342 -687 24 953 O ATOM 780 OD2 ASP A 150 221.666 19.598 75.459 1.00103.75 O ANISOU 780 OD2 ASP A 150 14346 11608 13466 -981 -194 1096 O ATOM 781 N ALA A 151 217.926 20.500 79.538 1.00 85.74 N ANISOU 781 N ALA A 151 12071 8994 11513 -46 -331 717 N ATOM 782 CA ALA A 151 217.493 21.337 80.653 1.00 80.29 C ANISOU 782 CA ALA A 151 11441 8214 10852 131 -443 614 C ATOM 783 C ALA A 151 217.295 20.515 81.919 1.00 70.07 C ANISOU 783 C ALA A 151 9971 7066 9585 220 -265 520 C ATOM 784 O ALA A 151 217.634 20.968 83.018 1.00 70.30 O ANISOU 784 O ALA A 151 10034 7060 9617 271 -288 478 O ATOM 785 CB ALA A 151 216.209 22.078 80.287 1.00 85.22 C ANISOU 785 CB ALA A 151 12123 8754 11501 318 -634 510 C ATOM 786 N CYS A 152 216.746 19.307 81.789 1.00 66.07 N ANISOU 786 N CYS A 152 9292 6723 9088 221 -98 492 N ATOM 787 CA CYS A 152 216.602 18.437 82.949 1.00 66.43 C ANISOU 787 CA CYS A 152 9196 6908 9135 249 57 431 C ATOM 788 C CYS A 152 217.930 17.824 83.369 1.00 65.00 C ANISOU 788 C CYS A 152 9018 6730 8949 106 161 525 C ATOM 789 O CYS A 152 218.123 17.522 84.552 1.00 68.44 O ANISOU 789 O CYS A 152 9410 7215 9379 120 227 492 O ATOM 790 CB CYS A 152 215.579 17.338 82.661 1.00 66.70 C ANISOU 790 CB CYS A 152 9073 7105 9164 265 173 382 C ATOM 791 SG CYS A 152 213.895 17.952 82.481 1.00 69.33 S ANISOU 791 SG CYS A 152 9344 7505 9491 463 69 214 S ATOM 792 N THR A 153 218.852 17.629 82.423 1.00 67.11 N ANISOU 792 N THR A 153 9325 6965 9207 -32 169 628 N ATOM 793 CA THR A 153 220.176 17.139 82.784 1.00 67.08 C ANISOU 793 CA THR A 153 9312 6981 9195 -146 243 685 C ATOM 794 C THR A 153 220.923 18.165 83.624 1.00 71.50 C ANISOU 794 C THR A 153 9982 7447 9738 -150 163 697 C ATOM 795 O THR A 153 221.629 17.806 84.574 1.00 74.33 O ANISOU 795 O THR A 153 10314 7830 10099 -169 226 695 O ATOM 796 CB THR A 153 220.970 16.789 81.527 1.00 64.88 C ANISOU 796 CB THR A 153 9022 6740 8890 -289 261 754 C ATOM 797 OG1 THR A 153 220.243 15.823 80.760 1.00 65.82 O ANISOU 797 OG1 THR A 153 9041 6939 9028 -276 330 735 O ATOM 798 CG2 THR A 153 222.326 16.212 81.898 1.00 63.19 C ANISOU 798 CG2 THR A 153 8764 6581 8664 -379 329 769 C ATOM 799 N TYR A 154 220.775 19.449 83.290 1.00 73.41 N ANISOU 799 N TYR A 154 10365 7565 9960 -134 4 710 N ATOM 800 CA TYR A 154 221.335 20.505 84.126 1.00 78.25 C ANISOU 800 CA TYR A 154 11105 8068 10558 -125 -100 712 C ATOM 801 C TYR A 154 220.727 20.475 85.522 1.00 79.28 C ANISOU 801 C TYR A 154 11175 8227 10720 35 -67 601 C ATOM 802 O TYR A 154 221.444 20.543 86.527 1.00 81.23 O ANISOU 802 O TYR A 154 11431 8470 10961 16 -35 602 O ATOM 803 CB TYR A 154 221.095 21.867 83.480 1.00 85.00 C ANISOU 803 CB TYR A 154 12153 8754 11388 -124 -324 738 C ATOM 804 CG TYR A 154 221.944 22.165 82.269 1.00 89.59 C ANISOU 804 CG TYR A 154 12837 9308 11896 -349 -386 869 C ATOM 805 CD1 TYR A 154 223.310 21.923 82.272 1.00 89.67 C ANISOU 805 CD1 TYR A 154 12827 9397 11845 -542 -307 942 C ATOM 806 CD2 TYR A 154 221.375 22.698 81.122 1.00 94.52 C ANISOU 806 CD2 TYR A 154 13571 9849 12494 -381 -533 909 C ATOM 807 CE1 TYR A 154 224.084 22.204 81.164 1.00 92.03 C ANISOU 807 CE1 TYR A 154 13194 9731 12044 -779 -357 1044 C ATOM 808 CE2 TYR A 154 222.137 22.975 80.011 1.00 96.86 C ANISOU 808 CE2 TYR A 154 13960 10150 12693 -628 -592 1033 C ATOM 809 CZ TYR A 154 223.489 22.731 80.038 1.00 97.71 C ANISOU 809 CZ TYR A 154 14028 10372 12725 -836 -497 1096 C ATOM 810 OH TYR A 154 224.244 23.018 78.927 1.00102.57 O ANISOU 810 OH TYR A 154 14712 11047 13212 -1112 -551 1203 O ATOM 811 N ALA A 155 219.397 20.374 85.600 1.00 78.75 N ANISOU 811 N ALA A 155 11032 8215 10674 184 -75 493 N ATOM 812 CA ALA A 155 218.718 20.412 86.891 1.00 78.97 C ANISOU 812 CA ALA A 155 10979 8323 10702 320 -48 360 C ATOM 813 C ALA A 155 219.206 19.300 87.810 1.00 77.69 C ANISOU 813 C ALA A 155 10711 8283 10525 236 126 386 C ATOM 814 O ALA A 155 219.378 19.512 89.015 1.00 82.33 O ANISOU 814 O ALA A 155 11290 8896 11096 268 137 336 O ATOM 815 CB ALA A 155 217.205 20.319 86.690 1.00 80.73 C ANISOU 815 CB ALA A 155 11096 8653 10926 466 -65 224 C ATOM 816 N THR A 156 219.437 18.107 87.262 1.00 73.06 N ANISOU 816 N THR A 156 10053 7764 9942 128 242 461 N ATOM 817 CA THR A 156 219.976 17.022 88.074 1.00 72.27 C ANISOU 817 CA THR A 156 9891 7737 9831 46 359 494 C ATOM 818 C THR A 156 221.404 17.326 88.513 1.00 69.73 C ANISOU 818 C THR A 156 9649 7330 9514 -23 341 560 C ATOM 819 O THR A 156 221.740 17.199 89.695 1.00 73.96 O ANISOU 819 O THR A 156 10180 7886 10035 -28 371 545 O ATOM 820 CB THR A 156 219.909 15.704 87.300 1.00 72.56 C ANISOU 820 CB THR A 156 9857 7835 9878 -33 443 544 C ATOM 821 OG1 THR A 156 218.538 15.340 87.094 1.00 75.02 O ANISOU 821 OG1 THR A 156 10082 8252 10169 13 472 480 O ATOM 822 CG2 THR A 156 220.614 14.592 88.064 1.00 73.41 C ANISOU 822 CG2 THR A 156 9943 7968 9981 -116 510 584 C ATOM 823 N ALA A 157 222.257 17.748 87.576 1.00 63.86 N ANISOU 823 N ALA A 157 8976 6512 8776 -93 291 629 N ATOM 824 CA ALA A 157 223.646 18.033 87.919 1.00 62.03 C ANISOU 824 CA ALA A 157 8801 6237 8530 -178 277 680 C ATOM 825 C ALA A 157 223.751 19.210 88.881 1.00 66.09 C ANISOU 825 C ALA A 157 9413 6668 9030 -126 193 653 C ATOM 826 O ALA A 157 224.543 19.174 89.830 1.00 72.68 O ANISOU 826 O ALA A 157 10256 7502 9857 -154 217 660 O ATOM 827 CB ALA A 157 224.459 18.300 86.653 1.00 60.24 C ANISOU 827 CB ALA A 157 8612 6000 8276 -300 239 746 C ATOM 828 N LEU A 158 222.958 20.261 88.658 1.00 66.84 N ANISOU 828 N LEU A 158 9587 6684 9125 -38 75 610 N ATOM 829 CA LEU A 158 223.009 21.418 89.545 1.00 66.26 C ANISOU 829 CA LEU A 158 9617 6516 9045 35 -37 561 C ATOM 830 C LEU A 158 222.465 21.082 90.928 1.00 71.54 C ANISOU 830 C LEU A 158 10188 7281 9713 135 36 458 C ATOM 831 O LEU A 158 222.978 21.581 91.936 1.00 77.62 O ANISOU 831 O LEU A 158 11004 8018 10471 146 11 439 O ATOM 832 CB LEU A 158 222.243 22.589 88.931 1.00 64.69 C ANISOU 832 CB LEU A 158 9540 6190 8851 130 -225 517 C ATOM 833 CG LEU A 158 222.859 23.193 87.668 1.00 67.16 C ANISOU 833 CG LEU A 158 10003 6384 9133 -12 -343 636 C ATOM 834 CD1 LEU A 158 221.991 24.320 87.129 1.00 68.96 C ANISOU 834 CD1 LEU A 158 10379 6453 9368 97 -571 588 C ATOM 835 CD2 LEU A 158 224.270 23.682 87.943 1.00 68.11 C ANISOU 835 CD2 LEU A 158 10229 6446 9203 -174 -373 729 C ATOM 836 N ASN A 159 221.428 20.243 91.000 1.00 69.61 N ANISOU 836 N ASN A 159 9809 7174 9467 187 125 393 N ATOM 837 CA ASN A 159 220.936 19.794 92.300 1.00 68.53 C ANISOU 837 CA ASN A 159 9567 7176 9293 222 206 306 C ATOM 838 C ASN A 159 222.009 19.011 93.045 1.00 65.50 C ANISOU 838 C ASN A 159 9182 6807 8898 98 295 395 C ATOM 839 O ASN A 159 222.331 19.319 94.198 1.00 66.41 O ANISOU 839 O ASN A 159 9311 6935 8988 104 294 363 O ATOM 840 CB ASN A 159 219.675 18.944 92.133 1.00 71.32 C ANISOU 840 CB ASN A 159 9779 7700 9618 244 285 238 C ATOM 841 CG ASN A 159 218.422 19.781 91.969 1.00 75.71 C ANISOU 841 CG ASN A 159 10292 8307 10165 413 193 76 C ATOM 842 OD1 ASN A 159 218.324 20.884 92.506 1.00 79.96 O ANISOU 842 OD1 ASN A 159 10878 8797 10705 537 79 -30 O ATOM 843 ND2 ASN A 159 217.454 19.256 91.227 1.00 74.22 N ANISOU 843 ND2 ASN A 159 10013 8219 9969 431 226 41 N ATOM 844 N VAL A 160 222.580 17.996 92.390 1.00 63.85 N ANISOU 844 N VAL A 160 8957 6595 8709 -5 358 493 N ATOM 845 CA VAL A 160 223.617 17.176 93.013 1.00 62.48 C ANISOU 845 CA VAL A 160 8785 6421 8533 -99 409 559 C ATOM 846 C VAL A 160 224.736 18.055 93.557 1.00 66.92 C ANISOU 846 C VAL A 160 9433 6897 9096 -111 357 580 C ATOM 847 O VAL A 160 225.276 17.804 94.643 1.00 70.61 O ANISOU 847 O VAL A 160 9905 7379 9546 -142 379 586 O ATOM 848 CB VAL A 160 224.142 16.135 92.006 1.00 59.77 C ANISOU 848 CB VAL A 160 8416 6071 8221 -169 440 625 C ATOM 849 CG1 VAL A 160 225.372 15.445 92.544 1.00 58.65 C ANISOU 849 CG1 VAL A 160 8288 5909 8089 -232 447 666 C ATOM 850 CG2 VAL A 160 223.062 15.114 91.704 1.00 60.29 C ANISOU 850 CG2 VAL A 160 8409 6220 8278 -176 490 611 C ATOM 851 N ALA A 161 225.083 19.114 92.827 1.00 67.76 N ANISOU 851 N ALA A 161 9621 6912 9211 -104 274 596 N ATOM 852 CA ALA A 161 226.035 20.086 93.351 1.00 67.99 C ANISOU 852 CA ALA A 161 9749 6860 9226 -130 207 615 C ATOM 853 C ALA A 161 225.432 20.870 94.511 1.00 71.32 C ANISOU 853 C ALA A 161 10196 7269 9632 -26 162 526 C ATOM 854 O ALA A 161 226.052 21.001 95.572 1.00 71.72 O ANISOU 854 O ALA A 161 10265 7320 9666 -45 174 523 O ATOM 855 CB ALA A 161 226.489 21.028 92.236 1.00 68.00 C ANISOU 855 CB ALA A 161 9856 6766 9215 -190 105 668 C ATOM 856 N SER A 162 224.213 21.387 94.333 1.00 75.20 N ANISOU 856 N SER A 162 10678 7768 10128 94 105 431 N ATOM 857 CA SER A 162 223.601 22.211 95.372 1.00 80.07 C ANISOU 857 CA SER A 162 11299 8398 10725 220 42 300 C ATOM 858 C SER A 162 223.241 21.398 96.608 1.00 81.29 C ANISOU 858 C SER A 162 11325 8729 10833 208 163 242 C ATOM 859 O SER A 162 223.210 21.945 97.716 1.00 81.74 O ANISOU 859 O SER A 162 11380 8819 10858 259 138 156 O ATOM 860 CB SER A 162 222.356 22.913 94.831 1.00 82.88 C ANISOU 860 CB SER A 162 11654 8742 11093 377 -69 177 C ATOM 861 OG SER A 162 221.298 21.991 94.628 1.00 85.10 O ANISOU 861 OG SER A 162 11781 9195 11359 400 32 120 O ATOM 862 N LEU A 163 222.950 20.104 96.444 1.00 82.66 N ANISOU 862 N LEU A 163 11400 9016 10990 125 278 288 N ATOM 863 CA LEU A 163 222.710 19.259 97.610 1.00 85.57 C ANISOU 863 CA LEU A 163 11682 9539 11291 55 372 266 C ATOM 864 C LEU A 163 223.943 19.202 98.503 1.00 82.78 C ANISOU 864 C LEU A 163 11395 9123 10933 -24 379 340 C ATOM 865 O LEU A 163 223.838 19.317 99.730 1.00 83.55 O ANISOU 865 O LEU A 163 11466 9310 10970 -36 397 283 O ATOM 866 CB LEU A 163 222.298 17.849 97.177 1.00 79.92 C ANISOU 866 CB LEU A 163 10898 8911 10557 -48 457 329 C ATOM 867 CG LEU A 163 220.807 17.500 97.128 1.00 80.68 C ANISOU 867 CG LEU A 163 10868 9200 10586 -31 500 227 C ATOM 868 CD1 LEU A 163 220.125 18.085 95.904 1.00 76.66 C ANISOU 868 CD1 LEU A 163 10346 8653 10130 93 447 169 C ATOM 869 CD2 LEU A 163 220.602 15.995 97.183 1.00 77.54 C ANISOU 869 CD2 LEU A 163 10435 8888 10138 -193 575 312 C ATOM 870 N SER A 164 225.125 19.036 97.904 1.00 82.61 N ANISOU 870 N SER A 164 11450 8972 10966 -81 362 453 N ATOM 871 CA SER A 164 226.352 19.004 98.688 1.00 84.29 C ANISOU 871 CA SER A 164 11717 9133 11176 -145 359 510 C ATOM 872 C SER A 164 226.773 20.390 99.158 1.00 84.22 C ANISOU 872 C SER A 164 11788 9047 11166 -89 284 469 C ATOM 873 O SER A 164 227.566 20.495 100.099 1.00 87.04 O ANISOU 873 O SER A 164 12177 9391 11503 -128 285 488 O ATOM 874 CB SER A 164 227.479 18.361 97.879 1.00 85.53 C ANISOU 874 CB SER A 164 11896 9223 11377 -215 360 606 C ATOM 875 OG SER A 164 227.827 19.158 96.761 1.00 89.76 O ANISOU 875 OG SER A 164 12479 9686 11941 -205 309 624 O ATOM 876 N VAL A 165 226.270 21.453 98.527 1.00 81.79 N ANISOU 876 N VAL A 165 11529 8673 10876 2 198 414 N ATOM 877 CA VAL A 165 226.573 22.799 99.002 1.00 78.21 C ANISOU 877 CA VAL A 165 11179 8120 10418 62 88 365 C ATOM 878 C VAL A 165 225.895 23.054 100.340 1.00 84.80 C ANISOU 878 C VAL A 165 11951 9062 11208 146 98 231 C ATOM 879 O VAL A 165 226.507 23.591 101.271 1.00 86.21 O ANISOU 879 O VAL A 165 12180 9209 11367 141 70 216 O ATOM 880 CB VAL A 165 226.164 23.846 97.950 1.00 73.41 C ANISOU 880 CB VAL A 165 10671 7382 9838 137 -54 340 C ATOM 881 CG1 VAL A 165 226.178 25.240 98.553 1.00 71.22 C ANISOU 881 CG1 VAL A 165 10514 6990 9555 233 -208 254 C ATOM 882 CG2 VAL A 165 227.097 23.779 96.758 1.00 73.33 C ANISOU 882 CG2 VAL A 165 10738 7284 9839 3 -73 480 C ATOM 883 N GLU A 166 224.622 22.670 100.461 1.00 87.25 N ANISOU 883 N GLU A 166 12137 9528 11486 212 142 120 N ATOM 884 CA GLU A 166 223.921 22.836 101.729 1.00 85.05 C ANISOU 884 CA GLU A 166 11759 9421 11134 268 166 -32 C ATOM 885 C GLU A 166 224.537 21.961 102.814 1.00 83.76 C ANISOU 885 C GLU A 166 11564 9350 10912 116 272 46 C ATOM 886 O GLU A 166 224.630 22.377 103.975 1.00 85.49 O ANISOU 886 O GLU A 166 11767 9639 11077 125 268 -31 O ATOM 887 CB GLU A 166 222.434 22.523 101.552 1.00 82.62 C ANISOU 887 CB GLU A 166 11299 9314 10779 340 200 -175 C ATOM 888 CG GLU A 166 221.684 22.214 102.842 1.00 85.56 C ANISOU 888 CG GLU A 166 11515 9967 11029 312 279 -317 C ATOM 889 CD GLU A 166 221.569 23.411 103.773 1.00 87.01 C ANISOU 889 CD GLU A 166 11689 10184 11187 457 188 -504 C ATOM 890 OE1 GLU A 166 221.906 24.541 103.358 1.00 90.07 O ANISOU 890 OE1 GLU A 166 12206 10357 11659 602 36 -537 O ATOM 891 OE2 GLU A 166 221.141 23.218 104.929 1.00 89.47 O ANISOU 891 OE2 GLU A 166 11870 10741 11382 412 255 -620 O ATOM 892 N ARG A 167 224.973 20.751 102.454 1.00 79.34 N ANISOU 892 N ARG A 167 11004 8783 10361 -21 347 191 N ATOM 893 CA ARG A 167 225.641 19.884 103.421 1.00 80.30 C ANISOU 893 CA ARG A 167 11131 8947 10433 -163 404 277 C ATOM 894 C ARG A 167 226.932 20.519 103.919 1.00 81.21 C ANISOU 894 C ARG A 167 11347 8928 10580 -166 357 326 C ATOM 895 O ARG A 167 227.222 20.508 105.121 1.00 82.11 O ANISOU 895 O ARG A 167 11460 9102 10636 -218 372 313 O ATOM 896 CB ARG A 167 225.922 18.518 102.797 1.00 76.14 C ANISOU 896 CB ARG A 167 10613 8390 9928 -274 442 408 C ATOM 897 CG ARG A 167 224.686 17.752 102.370 1.00 79.85 C ANISOU 897 CG ARG A 167 10992 8995 10351 -308 490 379 C ATOM 898 CD ARG A 167 225.071 16.460 101.671 1.00 75.91 C ANISOU 898 CD ARG A 167 10529 8423 9890 -400 495 506 C ATOM 899 NE ARG A 167 223.906 15.735 101.176 1.00 78.54 N ANISOU 899 NE ARG A 167 10790 8872 10178 -445 534 488 N ATOM 900 CZ ARG A 167 223.973 14.603 100.484 1.00 77.56 C ANISOU 900 CZ ARG A 167 10693 8697 10081 -515 527 576 C ATOM 901 NH1 ARG A 167 225.151 14.063 100.203 1.00 78.32 N ANISOU 901 NH1 ARG A 167 10872 8636 10251 -527 476 666 N ATOM 902 NH2 ARG A 167 222.860 14.010 100.074 1.00 77.62 N ANISOU 902 NH2 ARG A 167 10636 8820 10036 -566 562 557 N ATOM 903 N TYR A 168 227.727 21.071 103.000 1.00 82.28 N ANISOU 903 N TYR A 168 11569 8900 10794 -133 298 384 N ATOM 904 CA TYR A 168 228.948 21.770 103.390 1.00 83.99 C ANISOU 904 CA TYR A 168 11879 9007 11025 -152 248 425 C ATOM 905 C TYR A 168 228.634 22.948 104.302 1.00 81.17 C ANISOU 905 C TYR A 168 11549 8657 10636 -66 191 309 C ATOM 906 O TYR A 168 229.341 23.187 105.288 1.00 79.20 O ANISOU 906 O TYR A 168 11332 8401 10359 -103 187 316 O ATOM 907 CB TYR A 168 229.702 22.229 102.140 1.00 87.40 C ANISOU 907 CB TYR A 168 12389 9306 11511 -167 190 496 C ATOM 908 CG TYR A 168 230.831 23.203 102.402 1.00 89.44 C ANISOU 908 CG TYR A 168 12754 9465 11765 -203 119 526 C ATOM 909 CD1 TYR A 168 232.083 22.755 102.806 1.00 91.62 C ANISOU 909 CD1 TYR A 168 13031 9749 12031 -297 148 595 C ATOM 910 CD2 TYR A 168 230.650 24.571 102.226 1.00 89.02 C ANISOU 910 CD2 TYR A 168 12810 9303 11711 -144 0 480 C ATOM 911 CE1 TYR A 168 233.119 23.642 103.041 1.00 92.36 C ANISOU 911 CE1 TYR A 168 13213 9775 12105 -350 88 621 C ATOM 912 CE2 TYR A 168 231.680 25.464 102.458 1.00 89.35 C ANISOU 912 CE2 TYR A 168 12968 9248 11733 -207 -78 519 C ATOM 913 CZ TYR A 168 232.911 24.994 102.865 1.00 92.38 C ANISOU 913 CZ TYR A 168 13332 9671 12097 -318 -21 591 C ATOM 914 OH TYR A 168 233.940 25.878 103.098 1.00 95.35 O ANISOU 914 OH TYR A 168 13814 9976 12438 -399 -93 627 O ATOM 915 N LEU A 169 227.570 23.690 103.995 1.00 80.69 N ANISOU 915 N LEU A 169 11470 8610 10577 63 131 183 N ATOM 916 CA LEU A 169 227.151 24.790 104.854 1.00 79.44 C ANISOU 916 CA LEU A 169 11323 8471 10391 183 51 27 C ATOM 917 C LEU A 169 226.490 24.315 106.141 1.00 84.53 C ANISOU 917 C LEU A 169 11826 9350 10940 167 140 -82 C ATOM 918 O LEU A 169 226.244 25.138 107.025 1.00 84.44 O ANISOU 918 O LEU A 169 11798 9393 10891 256 88 -229 O ATOM 919 CB LEU A 169 226.197 25.715 104.095 1.00 77.94 C ANISOU 919 CB LEU A 169 11158 8221 10236 354 -78 -104 C ATOM 920 CG LEU A 169 226.821 26.612 103.026 1.00 75.44 C ANISOU 920 CG LEU A 169 11029 7651 9984 364 -228 -19 C ATOM 921 CD1 LEU A 169 225.756 27.464 102.354 1.00 76.47 C ANISOU 921 CD1 LEU A 169 11198 7712 10146 545 -388 -160 C ATOM 922 CD2 LEU A 169 227.910 27.487 103.626 1.00 76.13 C ANISOU 922 CD2 LEU A 169 11261 7600 10066 323 -315 20 C ATOM 923 N ALA A 170 226.196 23.022 106.271 1.00 84.37 N ANISOU 923 N ALA A 170 11711 9477 10870 41 260 -18 N ATOM 924 CA ALA A 170 225.564 22.495 107.474 1.00 85.89 C ANISOU 924 CA ALA A 170 11778 9918 10937 -37 341 -100 C ATOM 925 C ALA A 170 226.546 21.835 108.426 1.00 84.93 C ANISOU 925 C ALA A 170 11706 9790 10773 -202 386 29 C ATOM 926 O ALA A 170 226.335 21.877 109.642 1.00 88.46 O ANISOU 926 O ALA A 170 12093 10403 11115 -259 416 -47 O ATOM 927 CB ALA A 170 224.475 21.483 107.105 1.00 88.30 C ANISOU 927 CB ALA A 170 11963 10409 11179 -108 419 -115 C ATOM 928 N ILE A 171 227.610 21.233 107.907 1.00 81.45 N ANISOU 928 N ILE A 171 11364 9178 10405 -277 381 205 N ATOM 929 CA ILE A 171 228.587 20.520 108.720 1.00 78.28 C ANISOU 929 CA ILE A 171 11018 8750 9975 -414 394 323 C ATOM 930 C ILE A 171 229.842 21.353 108.947 1.00 80.49 C ANISOU 930 C ILE A 171 11394 8875 10312 -373 339 355 C ATOM 931 O ILE A 171 230.271 21.546 110.084 1.00 81.19 O ANISOU 931 O ILE A 171 11500 9001 10348 -419 337 344 O ATOM 932 CB ILE A 171 228.924 19.159 108.070 1.00 73.71 C ANISOU 932 CB ILE A 171 10471 8107 9430 -513 402 466 C ATOM 933 CG1 ILE A 171 227.682 18.269 108.027 1.00 75.31 C ANISOU 933 CG1 ILE A 171 10594 8473 9547 -599 450 448 C ATOM 934 CG2 ILE A 171 230.042 18.471 108.823 1.00 71.60 C ANISOU 934 CG2 ILE A 171 10281 7772 9152 -619 370 574 C ATOM 935 CD1 ILE A 171 227.893 16.961 107.293 1.00 72.63 C ANISOU 935 CD1 ILE A 171 10300 8050 9246 -679 431 574 C ATOM 936 N CYS A 172 230.438 21.868 107.869 1.00 83.80 N ANISOU 936 N CYS A 172 11879 9136 10826 -307 290 394 N ATOM 937 CA CYS A 172 231.682 22.620 107.987 1.00 90.07 C ANISOU 937 CA CYS A 172 12766 9803 11655 -308 236 435 C ATOM 938 C CYS A 172 231.479 24.009 108.580 1.00 92.80 C ANISOU 938 C CYS A 172 13152 10127 11980 -219 174 323 C ATOM 939 O CYS A 172 232.430 24.577 109.127 1.00 97.20 O ANISOU 939 O CYS A 172 13782 10617 12534 -246 136 347 O ATOM 940 CB CYS A 172 232.356 22.738 106.620 1.00 97.18 C ANISOU 940 CB CYS A 172 13716 10583 12626 -310 200 509 C ATOM 941 SG CYS A 172 232.896 21.162 105.921 1.00 99.98 S ANISOU 941 SG CYS A 172 14023 10952 13014 -388 243 612 S ATOM 942 N HIS A 173 230.275 24.569 108.487 1.00 92.57 N ANISOU 942 N HIS A 173 13078 10158 11938 -105 147 186 N ATOM 943 CA HIS A 173 229.995 25.916 108.981 1.00 94.15 C ANISOU 943 CA HIS A 173 13322 10323 12129 20 49 43 C ATOM 944 C HIS A 173 228.683 25.916 109.755 1.00 97.86 C ANISOU 944 C HIS A 173 13648 11013 12522 101 81 -147 C ATOM 945 O HIS A 173 227.606 26.072 109.156 1.00100.31 O ANISOU 945 O HIS A 173 13894 11379 12839 212 53 -261 O ATOM 946 CB HIS A 173 229.941 26.918 107.834 1.00 97.86 C ANISOU 946 CB HIS A 173 13909 10605 12668 116 -88 30 C ATOM 947 CG HIS A 173 231.189 27.728 107.683 1.00104.43 C ANISOU 947 CG HIS A 173 14907 11248 13523 55 -182 125 C ATOM 948 ND1 HIS A 173 231.425 28.873 108.413 1.00110.37 N ANISOU 948 ND1 HIS A 173 15757 11917 14261 116 -297 42 N ATOM 949 CD2 HIS A 173 232.274 27.556 106.891 1.00108.76 C ANISOU 949 CD2 HIS A 173 15532 11698 14092 -76 -182 284 C ATOM 950 CE1 HIS A 173 232.601 29.373 108.075 1.00112.03 C ANISOU 950 CE1 HIS A 173 16113 11977 14479 7 -364 165 C ATOM 951 NE2 HIS A 173 233.136 28.592 107.153 1.00110.77 N ANISOU 951 NE2 HIS A 173 15930 11824 14333 -116 -290 307 N ATOM 952 N PRO A 174 228.725 25.742 111.078 1.00 98.04 N ANISOU 952 N PRO A 174 13605 11190 12456 41 137 -199 N ATOM 953 CA PRO A 174 227.487 25.726 111.866 1.00 97.45 C ANISOU 953 CA PRO A 174 13362 11391 12272 86 178 -402 C ATOM 954 C PRO A 174 226.986 27.092 112.313 1.00102.42 C ANISOU 954 C PRO A 174 13975 12043 12896 290 61 -646 C ATOM 955 O PRO A 174 225.823 27.193 112.722 1.00104.95 O ANISOU 955 O PRO A 174 14128 12617 13133 373 75 -867 O ATOM 956 CB PRO A 174 227.873 24.874 113.094 1.00 95.12 C ANISOU 956 CB PRO A 174 13020 11255 11866 -112 282 -328 C ATOM 957 CG PRO A 174 229.221 24.267 112.768 1.00 96.89 C ANISOU 957 CG PRO A 174 13382 11267 12163 -232 288 -85 C ATOM 958 CD PRO A 174 229.869 25.249 111.856 1.00 98.22 C ANISOU 958 CD PRO A 174 13680 11186 12454 -110 185 -60 C ATOM 959 N PHE A 175 227.807 28.137 112.263 1.00106.21 N ANISOU 959 N PHE A 175 14619 12284 13453 370 -68 -630 N ATOM 960 CA PHE A 175 227.393 29.443 112.756 1.00112.29 C ANISOU 960 CA PHE A 175 15401 13043 14221 574 -217 -870 C ATOM 961 C PHE A 175 226.957 30.378 111.637 1.00113.68 C ANISOU 961 C PHE A 175 15690 13008 14496 772 -410 -952 C ATOM 962 O PHE A 175 226.459 31.473 111.920 1.00119.44 O ANISOU 962 O PHE A 175 16439 13706 15235 983 -581 -1183 O ATOM 963 CB PHE A 175 228.534 30.079 113.565 1.00112.40 C ANISOU 963 CB PHE A 175 15546 12922 14239 529 -269 -815 C ATOM 964 CG PHE A 175 228.076 31.093 114.579 1.00114.60 C ANISOU 964 CG PHE A 175 15777 13297 14470 697 -372 -1085 C ATOM 965 CD1 PHE A 175 227.045 30.794 115.456 1.00116.07 C ANISOU 965 CD1 PHE A 175 15725 13840 14536 734 -286 -1310 C ATOM 966 CD2 PHE A 175 228.702 32.324 114.685 1.00117.81 C ANISOU 966 CD2 PHE A 175 16372 13456 14936 799 -560 -1122 C ATOM 967 CE1 PHE A 175 226.628 31.712 116.401 1.00120.01 C ANISOU 967 CE1 PHE A 175 16152 14465 14982 900 -382 -1593 C ATOM 968 CE2 PHE A 175 228.291 33.247 115.629 1.00121.72 C ANISOU 968 CE2 PHE A 175 16825 14032 15392 972 -673 -1391 C ATOM 969 CZ PHE A 175 227.251 32.939 116.488 1.00123.16 C ANISOU 969 CZ PHE A 175 16745 14588 15461 1035 -581 -1639 C ATOM 970 N LYS A 176 227.127 29.967 110.380 1.00108.95 N ANISOU 970 N LYS A 176 15169 12262 13966 711 -404 -777 N ATOM 971 CA LYS A 176 226.715 30.745 109.221 1.00105.79 C ANISOU 971 CA LYS A 176 14892 11655 13649 861 -591 -822 C ATOM 972 C LYS A 176 225.406 30.258 108.617 1.00110.07 C ANISOU 972 C LYS A 176 15272 12365 14183 961 -555 -945 C ATOM 973 O LYS A 176 224.823 30.965 107.788 1.00115.22 O ANISOU 973 O LYS A 176 16002 12881 14896 1130 -734 -1042 O ATOM 974 CB LYS A 176 227.810 30.706 108.147 1.00101.34 C ANISOU 974 CB LYS A 176 14526 10829 13149 706 -622 -551 C ATOM 975 CG LYS A 176 228.329 32.063 107.709 1.00 99.01 C ANISOU 975 CG LYS A 176 14490 10226 12902 762 -875 -537 C ATOM 976 CD LYS A 176 229.416 31.897 106.659 1.00 96.04 C ANISOU 976 CD LYS A 176 14268 9674 12547 550 -872 -270 C ATOM 977 CE LYS A 176 230.725 32.523 107.109 1.00 94.98 C ANISOU 977 CE LYS A 176 14299 9398 12389 415 -935 -159 C ATOM 978 NZ LYS A 176 231.551 32.968 105.953 1.00 92.95 N ANISOU 978 NZ LYS A 176 14251 8935 12133 249 -1051 28 N ATOM 979 N ALA A 177 224.936 29.074 109.001 1.00107.53 N ANISOU 979 N ALA A 177 14745 12331 13782 848 -346 -938 N ATOM 980 CA ALA A 177 223.713 28.501 108.454 1.00104.96 C ANISOU 980 CA ALA A 177 14253 12199 13429 904 -291 -1041 C ATOM 981 C ALA A 177 222.563 28.470 109.444 1.00110.22 C ANISOU 981 C ALA A 177 14672 13236 13972 993 -241 -1331 C ATOM 982 O ALA A 177 221.434 28.782 109.068 1.00112.78 O ANISOU 982 O ALA A 177 14881 13681 14289 1176 -317 -1553 O ATOM 983 CB ALA A 177 223.974 27.078 107.949 1.00102.05 C ANISOU 983 CB ALA A 177 13846 11882 13046 677 -105 -804 C ATOM 984 N LYS A 178 222.824 28.117 110.706 1.00111.11 N ANISOU 984 N LYS A 178 14691 13552 13975 862 -124 -1347 N ATOM 985 CA LYS A 178 221.750 27.991 111.689 1.00113.96 C ANISOU 985 CA LYS A 178 14788 14334 14178 890 -54 -1622 C ATOM 986 C LYS A 178 220.891 29.248 111.777 1.00118.65 C ANISOU 986 C LYS A 178 15307 14988 14788 1218 -246 -1987 C ATOM 987 O LYS A 178 219.702 29.164 112.106 1.00122.75 O ANISOU 987 O LYS A 178 15572 15877 15191 1301 -215 -2267 O ATOM 988 CB LYS A 178 222.333 27.661 113.066 1.00111.13 C ANISOU 988 CB LYS A 178 14388 14135 13702 701 58 -1579 C ATOM 989 CG LYS A 178 222.971 26.285 113.168 1.00107.99 C ANISOU 989 CG LYS A 178 14030 13745 13255 382 228 -1271 C ATOM 990 CD LYS A 178 223.479 26.026 114.578 1.00105.24 C ANISOU 990 CD LYS A 178 13649 13557 12780 202 309 -1246 C ATOM 991 CE LYS A 178 224.052 24.626 114.716 1.00104.47 C ANISOU 991 CE LYS A 178 13609 13456 12629 -105 434 -956 C ATOM 992 NZ LYS A 178 224.551 24.370 116.096 1.00104.40 N ANISOU 992 NZ LYS A 178 13589 13588 12491 -291 490 -921 N ATOM 993 N THR A 179 221.463 30.416 111.472 1.00118.15 N ANISOU 993 N THR A 179 15462 14572 14857 1404 -464 -2003 N ATOM 994 CA THR A 179 220.738 31.673 111.588 1.00118.73 C ANISOU 994 CA THR A 179 15508 14643 14960 1741 -704 -2358 C ATOM 995 C THR A 179 220.432 32.348 110.258 1.00120.89 C ANISOU 995 C THR A 179 15951 14606 15376 1951 -937 -2376 C ATOM 996 O THR A 179 219.498 33.154 110.201 1.00125.87 O ANISOU 996 O THR A 179 16509 15296 16021 2253 -1138 -2709 O ATOM 997 CB THR A 179 221.519 32.661 112.469 1.00118.98 C ANISOU 997 CB THR A 179 15677 14517 15014 1817 -837 -2421 C ATOM 998 OG1 THR A 179 220.751 33.858 112.645 1.00121.22 O ANISOU 998 OG1 THR A 179 15926 14808 15322 2170 -1098 -2805 O ATOM 999 CG2 THR A 179 222.858 33.008 111.834 1.00114.33 C ANISOU 999 CG2 THR A 179 15430 13457 14554 1713 -930 -2092 C ATOM 1000 N LEU A 180 221.175 32.043 109.194 1.00118.73 N ANISOU 1000 N LEU A 180 15894 14020 15198 1804 -929 -2044 N ATOM 1001 CA LEU A 180 221.021 32.760 107.933 1.00116.59 C ANISOU 1001 CA LEU A 180 15828 13421 15050 1962 -1172 -2027 C ATOM 1002 C LEU A 180 220.097 32.070 106.939 1.00119.93 C ANISOU 1002 C LEU A 180 16126 13965 15477 1979 -1106 -2032 C ATOM 1003 O LEU A 180 219.453 32.756 106.138 1.00122.77 O ANISOU 1003 O LEU A 180 16561 14180 15908 2202 -1336 -2171 O ATOM 1004 CB LEU A 180 222.389 32.981 107.277 1.00113.00 C ANISOU 1004 CB LEU A 180 15691 12564 14679 1781 -1231 -1680 C ATOM 1005 CG LEU A 180 223.340 33.908 108.038 1.00111.34 C ANISOU 1005 CG LEU A 180 15669 12154 14482 1783 -1366 -1667 C ATOM 1006 CD1 LEU A 180 224.620 34.142 107.248 1.00106.80 C ANISOU 1006 CD1 LEU A 180 15393 11220 13965 1581 -1434 -1337 C ATOM 1007 CD2 LEU A 180 222.659 35.228 108.366 1.00112.40 C ANISOU 1007 CD2 LEU A 180 15859 12200 14647 2116 -1682 -2007 C ATOM 1008 N MET A 181 220.014 30.742 106.957 1.00118.24 N ANISOU 1008 N MET A 181 15741 13997 15188 1748 -822 -1885 N ATOM 1009 CA MET A 181 219.128 30.041 106.037 1.00116.03 C ANISOU 1009 CA MET A 181 15339 13845 14903 1748 -752 -1887 C ATOM 1010 C MET A 181 217.700 30.065 106.568 1.00118.04 C ANISOU 1010 C MET A 181 15289 14507 15052 1931 -746 -2266 C ATOM 1011 O MET A 181 217.454 29.762 107.740 1.00121.52 O ANISOU 1011 O MET A 181 15522 15291 15359 1867 -611 -2410 O ATOM 1012 CB MET A 181 219.606 28.602 105.811 1.00116.85 C ANISOU 1012 CB MET A 181 15402 14029 14966 1429 -482 -1584 C ATOM 1013 CG MET A 181 219.554 27.699 107.037 1.00119.66 C ANISOU 1013 CG MET A 181 15558 14733 15174 1237 -256 -1597 C ATOM 1014 SD MET A 181 218.170 26.546 107.093 1.00118.01 S ANISOU 1014 SD MET A 181 15037 14991 14811 1141 -70 -1725 S ATOM 1015 CE MET A 181 218.934 25.090 106.389 1.00116.98 C ANISOU 1015 CE MET A 181 15017 14724 14708 824 105 -1319 C ATOM 1016 N SER A 182 216.766 30.460 105.712 1.00115.46 N ANISOU 1016 N SER A 182 14931 14161 14775 2155 -904 -2441 N ATOM 1017 CA SER A 182 215.347 30.453 106.026 1.00116.36 C ANISOU 1017 CA SER A 182 14733 14690 14788 2342 -906 -2822 C ATOM 1018 C SER A 182 214.619 29.594 105.003 1.00111.22 C ANISOU 1018 C SER A 182 13980 14152 14126 2271 -802 -2749 C ATOM 1019 O SER A 182 215.196 29.150 104.007 1.00109.04 O ANISOU 1019 O SER A 182 13894 13597 13939 2121 -765 -2428 O ATOM 1020 CB SER A 182 214.771 31.876 106.044 1.00120.76 C ANISOU 1020 CB SER A 182 15325 15143 15414 2753 -1251 -3193 C ATOM 1021 OG SER A 182 214.831 32.470 104.758 1.00122.90 O ANISOU 1021 OG SER A 182 15859 14999 15839 2896 -1499 -3098 O ATOM 1022 N ARG A 183 213.333 29.351 105.260 1.00109.80 N ANISOU 1022 N ARG A 183 13481 14414 13823 2372 -751 -3065 N ATOM 1023 CA ARG A 183 212.531 28.625 104.284 1.00109.18 C ANISOU 1023 CA ARG A 183 13295 14459 13731 2331 -674 -3034 C ATOM 1024 C ARG A 183 212.397 29.412 102.988 1.00107.91 C ANISOU 1024 C ARG A 183 13347 13912 13744 2581 -947 -3035 C ATOM 1025 O ARG A 183 212.269 28.819 101.912 1.00108.20 O ANISOU 1025 O ARG A 183 13436 13851 13825 2484 -892 -2843 O ATOM 1026 CB ARG A 183 211.150 28.306 104.857 1.00104.76 C ANISOU 1026 CB ARG A 183 12333 14489 12982 2391 -582 -3409 C ATOM 1027 CG ARG A 183 210.854 26.819 104.953 1.00102.79 C ANISOU 1027 CG ARG A 183 11905 14581 12569 2020 -270 -3237 C ATOM 1028 CD ARG A 183 209.423 26.567 105.394 1.00100.98 C ANISOU 1028 CD ARG A 183 11273 14963 12132 2062 -195 -3621 C ATOM 1029 NE ARG A 183 208.467 26.920 104.348 1.00101.76 N ANISOU 1029 NE ARG A 183 11300 15065 12301 2334 -349 -3823 N ATOM 1030 CZ ARG A 183 207.147 26.875 104.495 1.00104.09 C ANISOU 1030 CZ ARG A 183 11242 15866 12442 2448 -337 -4206 C ATOM 1031 NH1 ARG A 183 206.619 26.490 105.648 1.00105.39 N ANISOU 1031 NH1 ARG A 183 11086 16601 12356 2288 -170 -4428 N ATOM 1032 NH2 ARG A 183 206.355 27.215 103.487 1.00104.70 N ANISOU 1032 NH2 ARG A 183 11280 15900 12602 2709 -497 -4373 N ATOM 1033 N SER A 184 212.441 30.744 103.070 1.00109.32 N ANISOU 1033 N SER A 184 13666 13854 14017 2892 -1260 -3242 N ATOM 1034 CA SER A 184 212.310 31.566 101.872 1.00110.20 C ANISOU 1034 CA SER A 184 14018 13570 14282 3120 -1570 -3242 C ATOM 1035 C SER A 184 213.578 31.526 101.029 1.00108.04 C ANISOU 1035 C SER A 184 14112 12814 14122 2898 -1587 -2790 C ATOM 1036 O SER A 184 213.505 31.455 99.796 1.00112.13 O ANISOU 1036 O SER A 184 14772 13114 14716 2884 -1667 -2636 O ATOM 1037 CB SER A 184 211.969 33.004 102.258 1.00113.67 C ANISOU 1037 CB SER A 184 14525 13884 14780 3518 -1944 -3611 C ATOM 1038 OG SER A 184 211.891 33.832 101.111 1.00115.89 O ANISOU 1038 OG SER A 184 15091 13738 15205 3719 -2289 -3589 O ATOM 1039 N ARG A 185 214.748 31.576 101.671 1.00104.17 N ANISOU 1039 N ARG A 185 13768 12179 13635 2716 -1512 -2587 N ATOM 1040 CA ARG A 185 216.002 31.554 100.924 1.00101.27 C ANISOU 1040 CA ARG A 185 13719 11408 13351 2491 -1522 -2186 C ATOM 1041 C ARG A 185 216.163 30.240 100.170 1.00101.51 C ANISOU 1041 C ARG A 185 13686 11523 13361 2213 -1251 -1902 C ATOM 1042 O ARG A 185 216.457 30.230 98.969 1.00100.51 O ANISOU 1042 O ARG A 185 13743 11140 13306 2143 -1322 -1695 O ATOM 1043 CB ARG A 185 217.184 31.778 101.867 1.00103.37 C ANISOU 1043 CB ARG A 185 14102 11570 13603 2348 -1471 -2054 C ATOM 1044 CG ARG A 185 218.484 32.115 101.151 1.00102.14 C ANISOU 1044 CG ARG A 185 14292 10993 13525 2166 -1562 -1713 C ATOM 1045 CD ARG A 185 219.708 31.713 101.962 1.00100.97 C ANISOU 1045 CD ARG A 185 14175 10852 13337 1916 -1369 -1504 C ATOM 1046 NE ARG A 185 219.972 30.280 101.857 1.00 95.39 N ANISOU 1046 NE ARG A 185 13318 10346 12582 1655 -1045 -1295 N ATOM 1047 CZ ARG A 185 221.177 29.731 101.971 1.00 88.19 C ANISOU 1047 CZ ARG A 185 12485 9360 11662 1400 -893 -1025 C ATOM 1048 NH1 ARG A 185 222.237 30.497 102.192 1.00 90.46 N ANISOU 1048 NH1 ARG A 185 12988 9405 11977 1347 -1012 -922 N ATOM 1049 NH2 ARG A 185 221.323 28.417 101.858 1.00 81.08 N ANISOU 1049 NH2 ARG A 185 11455 8629 10725 1200 -642 -868 N ATOM 1050 N THR A 186 215.968 29.116 100.864 1.00102.03 N ANISOU 1050 N THR A 186 13500 11948 13319 2042 -953 -1892 N ATOM 1051 CA THR A 186 216.088 27.814 100.217 1.00 98.20 C ANISOU 1051 CA THR A 186 12959 11541 12812 1788 -716 -1641 C ATOM 1052 C THR A 186 215.010 27.619 99.157 1.00 94.50 C ANISOU 1052 C THR A 186 12404 11142 12360 1899 -763 -1732 C ATOM 1053 O THR A 186 215.236 26.923 98.161 1.00 91.71 O ANISOU 1053 O THR A 186 12115 10688 12043 1744 -677 -1501 O ATOM 1054 CB THR A 186 216.029 26.703 101.272 1.00 97.92 C ANISOU 1054 CB THR A 186 12700 11864 12641 1579 -437 -1628 C ATOM 1055 OG1 THR A 186 217.061 26.912 102.247 1.00 95.80 O ANISOU 1055 OG1 THR A 186 12524 11516 12361 1482 -407 -1540 O ATOM 1056 CG2 THR A 186 216.227 25.332 100.636 1.00 99.32 C ANISOU 1056 CG2 THR A 186 12856 12080 12801 1316 -227 -1364 C ATOM 1057 N LYS A 187 213.845 28.243 99.339 1.00 93.28 N ANISOU 1057 N LYS A 187 12097 11164 12180 2178 -910 -2083 N ATOM 1058 CA LYS A 187 212.772 28.126 98.356 1.00 93.67 C ANISOU 1058 CA LYS A 187 12054 11290 12245 2310 -976 -2200 C ATOM 1059 C LYS A 187 213.202 28.697 97.009 1.00 93.15 C ANISOU 1059 C LYS A 187 12292 10785 12317 2354 -1191 -2013 C ATOM 1060 O LYS A 187 213.223 27.990 95.995 1.00 93.49 O ANISOU 1060 O LYS A 187 12366 10774 12381 2206 -1095 -1808 O ATOM 1061 CB LYS A 187 211.517 28.836 98.866 1.00 93.98 C ANISOU 1061 CB LYS A 187 11873 11600 12234 2641 -1136 -2657 C ATOM 1062 CG LYS A 187 210.209 28.164 98.482 1.00 93.99 C ANISOU 1062 CG LYS A 187 11587 11975 12151 2683 -1037 -2840 C ATOM 1063 CD LYS A 187 209.737 27.222 99.578 1.00 94.36 C ANISOU 1063 CD LYS A 187 11301 12548 12003 2497 -748 -2952 C ATOM 1064 CE LYS A 187 208.390 26.606 99.238 1.00 93.88 C ANISOU 1064 CE LYS A 187 10940 12900 11831 2522 -658 -3159 C ATOM 1065 NZ LYS A 187 207.845 25.796 100.363 1.00 95.13 N ANISOU 1065 NZ LYS A 187 10770 13614 11761 2321 -408 -3301 N ATOM 1066 N LYS A 188 213.561 29.984 96.985 1.00 94.93 N ANISOU 1066 N LYS A 188 12756 10690 12623 2538 -1498 -2079 N ATOM 1067 CA LYS A 188 213.911 30.627 95.723 1.00 94.64 C ANISOU 1067 CA LYS A 188 13030 10238 12689 2558 -1745 -1911 C ATOM 1068 C LYS A 188 215.247 30.130 95.185 1.00 94.05 C ANISOU 1068 C LYS A 188 13155 9949 12633 2215 -1603 -1498 C ATOM 1069 O LYS A 188 215.469 30.149 93.969 1.00 92.97 O ANISOU 1069 O LYS A 188 13191 9594 12539 2124 -1685 -1307 O ATOM 1070 CB LYS A 188 213.933 32.147 95.897 1.00 95.60 C ANISOU 1070 CB LYS A 188 13384 10061 12877 2826 -2148 -2092 C ATOM 1071 CG LYS A 188 214.099 32.917 94.596 1.00 94.41 C ANISOU 1071 CG LYS A 188 13574 9485 12811 2856 -2469 -1953 C ATOM 1072 CD LYS A 188 214.059 34.417 94.825 1.00 95.06 C ANISOU 1072 CD LYS A 188 13913 9253 12954 3128 -2914 -2147 C ATOM 1073 CE LYS A 188 214.251 35.175 93.522 1.00 97.16 C ANISOU 1073 CE LYS A 188 14560 9075 13283 3110 -3263 -1978 C ATOM 1074 NZ LYS A 188 214.210 36.649 93.726 1.00100.22 N ANISOU 1074 NZ LYS A 188 15245 9108 13727 3369 -3749 -2158 N ATOM 1075 N PHE A 189 216.144 29.683 96.069 1.00 94.63 N ANISOU 1075 N PHE A 189 13194 10098 12663 2024 -1399 -1371 N ATOM 1076 CA PHE A 189 217.412 29.114 95.619 1.00 94.99 C ANISOU 1076 CA PHE A 189 13378 9999 12715 1713 -1251 -1019 C ATOM 1077 C PHE A 189 217.184 27.953 94.660 1.00 95.88 C ANISOU 1077 C PHE A 189 13386 10224 12819 1558 -1056 -867 C ATOM 1078 O PHE A 189 217.929 27.784 93.688 1.00 96.24 O ANISOU 1078 O PHE A 189 13587 10089 12891 1380 -1054 -625 O ATOM 1079 CB PHE A 189 218.235 28.665 96.827 1.00 98.46 C ANISOU 1079 CB PHE A 189 13744 10563 13104 1564 -1050 -954 C ATOM 1080 CG PHE A 189 219.542 28.009 96.472 1.00100.63 C ANISOU 1080 CG PHE A 189 14121 10734 13380 1271 -896 -637 C ATOM 1081 CD1 PHE A 189 219.621 26.637 96.285 1.00 98.52 C ANISOU 1081 CD1 PHE A 189 13701 10650 13083 1093 -636 -508 C ATOM 1082 CD2 PHE A 189 220.695 28.764 96.339 1.00104.49 C ANISOU 1082 CD2 PHE A 189 14856 10955 13890 1171 -1026 -485 C ATOM 1083 CE1 PHE A 189 220.824 26.033 95.967 1.00 96.39 C ANISOU 1083 CE1 PHE A 189 13507 10301 12817 859 -518 -260 C ATOM 1084 CE2 PHE A 189 221.901 28.165 96.020 1.00103.05 C ANISOU 1084 CE2 PHE A 189 14732 10728 13695 911 -885 -232 C ATOM 1085 CZ PHE A 189 221.964 26.798 95.833 1.00 98.55 C ANISOU 1085 CZ PHE A 189 13993 10346 13107 773 -635 -133 C ATOM 1086 N ILE A 190 216.154 27.145 94.915 1.00 93.67 N ANISOU 1086 N ILE A 190 12838 10262 12490 1611 -897 -1015 N ATOM 1087 CA ILE A 190 215.845 26.027 94.032 1.00 85.06 C ANISOU 1087 CA ILE A 190 11648 9281 11389 1473 -726 -888 C ATOM 1088 C ILE A 190 215.183 26.517 92.752 1.00 86.65 C ANISOU 1088 C ILE A 190 11938 9338 11646 1603 -919 -922 C ATOM 1089 O ILE A 190 215.457 26.002 91.663 1.00 86.44 O ANISOU 1089 O ILE A 190 11978 9223 11643 1457 -866 -726 O ATOM 1090 CB ILE A 190 214.969 25.002 94.772 1.00 79.54 C ANISOU 1090 CB ILE A 190 10651 8977 10595 1446 -504 -1023 C ATOM 1091 CG1 ILE A 190 215.701 24.490 96.008 1.00 80.16 C ANISOU 1091 CG1 ILE A 190 10677 9170 10610 1284 -333 -956 C ATOM 1092 CG2 ILE A 190 214.613 23.845 93.861 1.00 79.21 C ANISOU 1092 CG2 ILE A 190 10522 9034 10540 1304 -348 -895 C ATOM 1093 CD1 ILE A 190 214.809 23.781 96.968 1.00 82.28 C ANISOU 1093 CD1 ILE A 190 10678 9834 10752 1254 -173 -1126 C ATOM 1094 N SER A 191 214.306 27.520 92.860 1.00 87.82 N ANISOU 1094 N SER A 191 12091 9462 11815 1888 -1161 -1186 N ATOM 1095 CA SER A 191 213.691 28.092 91.667 1.00 92.80 C ANISOU 1095 CA SER A 191 12841 9917 12502 2030 -1397 -1226 C ATOM 1096 C SER A 191 214.736 28.678 90.729 1.00 92.50 C ANISOU 1096 C SER A 191 13139 9492 12514 1882 -1564 -959 C ATOM 1097 O SER A 191 214.558 28.651 89.505 1.00 97.43 O ANISOU 1097 O SER A 191 13864 9993 13163 1838 -1647 -852 O ATOM 1098 CB SER A 191 212.671 29.162 92.059 1.00 96.72 C ANISOU 1098 CB SER A 191 13304 10426 13017 2392 -1680 -1584 C ATOM 1099 OG SER A 191 211.629 28.614 92.847 1.00100.46 O ANISOU 1099 OG SER A 191 13431 11324 13415 2510 -1521 -1858 O ATOM 1100 N ALA A 192 215.831 29.208 91.279 1.00 87.97 N ANISOU 1100 N ALA A 192 12739 8745 11941 1783 -1615 -849 N ATOM 1101 CA ALA A 192 216.914 29.698 90.437 1.00 79.86 C ANISOU 1101 CA ALA A 192 12014 7404 10924 1578 -1748 -583 C ATOM 1102 C ALA A 192 217.660 28.554 89.764 1.00 75.14 C ANISOU 1102 C ALA A 192 11358 6897 10296 1274 -1473 -319 C ATOM 1103 O ALA A 192 218.142 28.711 88.637 1.00 78.31 O ANISOU 1103 O ALA A 192 11935 7131 10689 1109 -1558 -131 O ATOM 1104 CB ALA A 192 217.878 30.551 91.261 1.00 80.82 C ANISOU 1104 CB ALA A 192 12320 7348 11038 1541 -1868 -550 C ATOM 1105 N ILE A 193 217.765 27.404 90.434 1.00 70.48 N ANISOU 1105 N ILE A 193 10528 6572 9679 1192 -1164 -310 N ATOM 1106 CA ILE A 193 218.433 26.251 89.833 1.00 70.17 C ANISOU 1106 CA ILE A 193 10423 6620 9619 941 -927 -97 C ATOM 1107 C ILE A 193 217.704 25.818 88.570 1.00 71.56 C ANISOU 1107 C ILE A 193 10560 6823 9808 941 -928 -71 C ATOM 1108 O ILE A 193 218.321 25.565 87.528 1.00 77.82 O ANISOU 1108 O ILE A 193 11439 7537 10590 753 -908 115 O ATOM 1109 CB ILE A 193 218.532 25.097 90.846 1.00 73.26 C ANISOU 1109 CB ILE A 193 10587 7267 9981 879 -646 -115 C ATOM 1110 CG1 ILE A 193 219.426 25.487 92.023 1.00 74.44 C ANISOU 1110 CG1 ILE A 193 10791 7378 10114 844 -639 -107 C ATOM 1111 CG2 ILE A 193 219.057 23.840 90.172 1.00 72.58 C ANISOU 1111 CG2 ILE A 193 10429 7264 9885 669 -440 65 C ATOM 1112 CD1 ILE A 193 219.506 24.429 93.095 1.00 75.85 C ANISOU 1112 CD1 ILE A 193 10777 7790 10253 778 -402 -125 C ATOM 1113 N TRP A 194 216.375 25.730 88.642 1.00 70.29 N ANISOU 1113 N TRP A 194 10250 6799 9657 1146 -950 -272 N ATOM 1114 CA TRP A 194 215.603 25.342 87.469 1.00 70.07 C ANISOU 1114 CA TRP A 194 10177 6804 9641 1161 -957 -262 C ATOM 1115 C TRP A 194 215.583 26.444 86.418 1.00 70.37 C ANISOU 1115 C TRP A 194 10472 6558 9706 1203 -1263 -218 C ATOM 1116 O TRP A 194 215.579 26.152 85.217 1.00 72.76 O ANISOU 1116 O TRP A 194 10826 6814 10006 1088 -1265 -88 O ATOM 1117 CB TRP A 194 214.181 24.965 87.880 1.00 72.38 C ANISOU 1117 CB TRP A 194 10226 7354 9920 1362 -901 -507 C ATOM 1118 CG TRP A 194 214.099 23.645 88.577 1.00 76.61 C ANISOU 1118 CG TRP A 194 10526 8181 10403 1241 -598 -499 C ATOM 1119 CD1 TRP A 194 214.274 23.412 89.909 1.00 78.77 C ANISOU 1119 CD1 TRP A 194 10690 8608 10630 1227 -480 -571 C ATOM 1120 CD2 TRP A 194 213.817 22.373 87.980 1.00 78.02 C ANISOU 1120 CD2 TRP A 194 10570 8516 10559 1101 -398 -407 C ATOM 1121 NE1 TRP A 194 214.123 22.073 90.179 1.00 80.75 N ANISOU 1121 NE1 TRP A 194 10765 9091 10824 1072 -235 -518 N ATOM 1122 CE2 TRP A 194 213.842 21.414 89.011 1.00 78.81 C ANISOU 1122 CE2 TRP A 194 10505 8843 10596 999 -185 -420 C ATOM 1123 CE3 TRP A 194 213.548 21.953 86.674 1.00 75.56 C ANISOU 1123 CE3 TRP A 194 10273 8167 10268 1045 -392 -314 C ATOM 1124 CZ2 TRP A 194 213.606 20.060 88.778 1.00 78.40 C ANISOU 1124 CZ2 TRP A 194 10325 8960 10505 843 11 -340 C ATOM 1125 CZ3 TRP A 194 213.315 20.607 86.444 1.00 75.04 C ANISOU 1125 CZ3 TRP A 194 10056 8284 10170 907 -178 -247 C ATOM 1126 CH2 TRP A 194 213.346 19.677 87.491 1.00 76.68 C ANISOU 1126 CH2 TRP A 194 10122 8695 10318 808 10 -260 C ATOM 1127 N LEU A 195 215.576 27.710 86.844 1.00 69.76 N ANISOU 1127 N LEU A 195 10574 6282 9649 1357 -1539 -321 N ATOM 1128 CA LEU A 195 215.559 28.806 85.881 1.00 68.57 C ANISOU 1128 CA LEU A 195 10716 5822 9514 1381 -1882 -269 C ATOM 1129 C LEU A 195 216.875 28.889 85.118 1.00 72.53 C ANISOU 1129 C LEU A 195 11434 6158 9965 1046 -1885 32 C ATOM 1130 O LEU A 195 216.880 29.084 83.898 1.00 76.44 O ANISOU 1130 O LEU A 195 12080 6524 10438 928 -2014 160 O ATOM 1131 CB LEU A 195 215.265 30.127 86.590 1.00 68.62 C ANISOU 1131 CB LEU A 195 10883 5635 9553 1633 -2210 -464 C ATOM 1132 CG LEU A 195 215.351 31.387 85.728 1.00 69.32 C ANISOU 1132 CG LEU A 195 11346 5341 9652 1646 -2634 -399 C ATOM 1133 CD1 LEU A 195 214.348 31.333 84.585 1.00 68.39 C ANISOU 1133 CD1 LEU A 195 11232 5196 9556 1749 -2767 -445 C ATOM 1134 CD2 LEU A 195 215.139 32.631 86.577 1.00 72.20 C ANISOU 1134 CD2 LEU A 195 11871 5508 10056 1908 -2965 -609 C ATOM 1135 N ALA A 196 218.000 28.744 85.819 1.00 73.70 N ANISOU 1135 N ALA A 196 11588 6333 10081 878 -1745 137 N ATOM 1136 CA ALA A 196 219.291 28.775 85.143 1.00 74.37 C ANISOU 1136 CA ALA A 196 11833 6329 10095 546 -1726 394 C ATOM 1137 C ALA A 196 219.489 27.550 84.261 1.00 78.56 C ANISOU 1137 C ALA A 196 12195 7056 10599 359 -1467 519 C ATOM 1138 O ALA A 196 220.152 27.637 83.222 1.00 78.97 O ANISOU 1138 O ALA A 196 12372 7050 10581 112 -1510 695 O ATOM 1139 CB ALA A 196 220.422 28.883 86.167 1.00 75.02 C ANISOU 1139 CB ALA A 196 11932 6422 10148 434 -1635 447 C ATOM 1140 N SER A 197 218.921 26.407 84.652 1.00 81.71 N ANISOU 1140 N SER A 197 12314 7695 11037 460 -1211 423 N ATOM 1141 CA SER A 197 219.061 25.201 83.844 1.00 82.77 C ANISOU 1141 CA SER A 197 12294 8002 11155 307 -986 522 C ATOM 1142 C SER A 197 218.318 25.325 82.520 1.00 82.58 C ANISOU 1142 C SER A 197 12328 7920 11128 313 -1107 545 C ATOM 1143 O SER A 197 218.771 24.786 81.503 1.00 82.94 O ANISOU 1143 O SER A 197 12360 8022 11130 111 -1021 680 O ATOM 1144 CB SER A 197 218.560 23.985 84.623 1.00 86.27 C ANISOU 1144 CB SER A 197 12461 8686 11630 403 -725 418 C ATOM 1145 OG SER A 197 217.183 24.107 84.931 1.00 88.56 O ANISOU 1145 OG SER A 197 12657 9036 11956 646 -781 228 O ATOM 1146 N ALA A 198 217.182 26.028 82.511 1.00 81.00 N ANISOU 1146 N ALA A 198 12186 7621 10970 549 -1316 399 N ATOM 1147 CA ALA A 198 216.438 26.209 81.270 1.00 78.01 C ANISOU 1147 CA ALA A 198 11879 7169 10591 570 -1463 414 C ATOM 1148 C ALA A 198 217.121 27.209 80.347 1.00 76.06 C ANISOU 1148 C ALA A 198 11950 6671 10280 371 -1727 587 C ATOM 1149 O ALA A 198 217.031 27.081 79.121 1.00 77.85 O ANISOU 1149 O ALA A 198 12235 6879 10465 232 -1770 695 O ATOM 1150 CB ALA A 198 215.009 26.654 81.575 1.00 76.32 C ANISOU 1150 CB ALA A 198 11616 6942 10439 906 -1627 173 C ATOM 1151 N LEU A 199 217.804 28.207 80.911 1.00 75.44 N ANISOU 1151 N LEU A 199 12085 6403 10176 331 -1913 620 N ATOM 1152 CA LEU A 199 218.514 29.173 80.079 1.00 75.44 C ANISOU 1152 CA LEU A 199 12412 6167 10084 86 -2179 804 C ATOM 1153 C LEU A 199 219.741 28.544 79.430 1.00 74.76 C ANISOU 1153 C LEU A 199 12283 6236 9887 -294 -1970 1014 C ATOM 1154 O LEU A 199 220.072 28.859 78.281 1.00 79.51 O ANISOU 1154 O LEU A 199 13052 6771 10386 -547 -2098 1172 O ATOM 1155 CB LEU A 199 218.911 30.392 80.911 1.00 76.63 C ANISOU 1155 CB LEU A 199 12811 6075 10231 137 -2444 779 C ATOM 1156 CG LEU A 199 217.763 31.237 81.467 1.00 80.14 C ANISOU 1156 CG LEU A 199 13342 6335 10773 521 -2735 546 C ATOM 1157 CD1 LEU A 199 218.298 32.345 82.361 1.00 80.75 C ANISOU 1157 CD1 LEU A 199 13651 6184 10844 558 -2974 519 C ATOM 1158 CD2 LEU A 199 216.919 31.812 80.340 1.00 81.50 C ANISOU 1158 CD2 LEU A 199 13711 6306 10948 589 -3054 544 C ATOM 1159 N LEU A 200 220.425 27.650 80.146 1.00 69.97 N ANISOU 1159 N LEU A 200 11448 5850 9288 -342 -1661 1005 N ATOM 1160 CA LEU A 200 221.610 27.010 79.591 1.00 66.72 C ANISOU 1160 CA LEU A 200 10958 5618 8774 -664 -1467 1154 C ATOM 1161 C LEU A 200 221.273 26.038 78.469 1.00 64.43 C ANISOU 1161 C LEU A 200 10506 5503 8471 -736 -1314 1182 C ATOM 1162 O LEU A 200 222.156 25.704 77.672 1.00 69.69 O ANISOU 1162 O LEU A 200 11145 6307 9028 -1021 -1227 1298 O ATOM 1163 CB LEU A 200 222.383 26.283 80.691 1.00 67.57 C ANISOU 1163 CB LEU A 200 10867 5899 8907 -653 -1210 1111 C ATOM 1164 CG LEU A 200 223.082 27.138 81.749 1.00 65.36 C ANISOU 1164 CG LEU A 200 10730 5495 8611 -664 -1315 1114 C ATOM 1165 CD1 LEU A 200 223.660 26.255 82.840 1.00 63.39 C ANISOU 1165 CD1 LEU A 200 10255 5428 8401 -616 -1048 1054 C ATOM 1166 CD2 LEU A 200 224.167 27.989 81.114 1.00 66.52 C ANISOU 1166 CD2 LEU A 200 11111 5559 8605 -1004 -1479 1286 C ATOM 1167 N ALA A 201 220.027 25.575 78.390 1.00 57.58 N ANISOU 1167 N ALA A 201 9518 4659 7702 -491 -1280 1065 N ATOM 1168 CA ALA A 201 219.602 24.668 77.333 1.00 57.49 C ANISOU 1168 CA ALA A 201 9361 4798 7685 -542 -1148 1084 C ATOM 1169 C ALA A 201 219.000 25.398 76.142 1.00 57.48 C ANISOU 1169 C ALA A 201 9559 4641 7638 -596 -1402 1148 C ATOM 1170 O ALA A 201 218.593 24.745 75.174 1.00 57.36 O ANISOU 1170 O ALA A 201 9444 4737 7612 -644 -1319 1169 O ATOM 1171 CB ALA A 201 218.597 23.650 77.882 1.00 58.40 C ANISOU 1171 CB ALA A 201 9223 5055 7913 -282 -955 929 C ATOM 1172 N ILE A 202 218.933 26.730 76.192 1.00 58.37 N ANISOU 1172 N ILE A 202 9968 4485 7723 -591 -1729 1181 N ATOM 1173 CA ILE A 202 218.393 27.495 75.064 1.00 65.34 C ANISOU 1173 CA ILE A 202 11091 5180 8557 -655 -2025 1256 C ATOM 1174 C ILE A 202 219.153 27.234 73.767 1.00 73.55 C ANISOU 1174 C ILE A 202 12164 6337 9442 -1044 -1975 1443 C ATOM 1175 O ILE A 202 218.509 27.110 72.716 1.00 75.89 O ANISOU 1175 O ILE A 202 12483 6631 9721 -1070 -2043 1473 O ATOM 1176 CB ILE A 202 218.305 28.981 75.422 1.00 66.09 C ANISOU 1176 CB ILE A 202 11534 4935 8645 -592 -2424 1260 C ATOM 1177 CG1 ILE A 202 217.273 29.201 76.532 1.00 63.49 C ANISOU 1177 CG1 ILE A 202 11131 4525 8469 -155 -2493 1018 C ATOM 1178 CG2 ILE A 202 217.958 29.818 74.202 1.00 65.85 C ANISOU 1178 CG2 ILE A 202 11810 4676 8533 -728 -2775 1377 C ATOM 1179 CD1 ILE A 202 215.852 28.898 76.112 1.00 62.42 C ANISOU 1179 CD1 ILE A 202 10878 4417 8422 121 -2533 866 C ATOM 1180 N PRO A 203 220.508 27.145 73.749 1.00 75.40 N ANISOU 1180 N PRO A 203 12391 6707 9550 -1361 -1859 1561 N ATOM 1181 CA PRO A 203 221.206 26.884 72.479 1.00 76.69 C ANISOU 1181 CA PRO A 203 12551 7045 9543 -1742 -1807 1707 C ATOM 1182 C PRO A 203 220.736 25.643 71.731 1.00 76.32 C ANISOU 1182 C PRO A 203 12226 7237 9534 -1694 -1562 1651 C ATOM 1183 O PRO A 203 220.918 25.554 70.512 1.00 80.17 O ANISOU 1183 O PRO A 203 12739 7828 9893 -1955 -1584 1751 O ATOM 1184 CB PRO A 203 222.668 26.737 72.915 1.00 77.40 C ANISOU 1184 CB PRO A 203 12563 7323 9523 -1993 -1648 1757 C ATOM 1185 CG PRO A 203 222.775 27.615 74.095 1.00 75.87 C ANISOU 1185 CG PRO A 203 12543 6898 9385 -1859 -1807 1733 C ATOM 1186 CD PRO A 203 221.465 27.487 74.820 1.00 75.90 C ANISOU 1186 CD PRO A 203 12486 6757 9594 -1412 -1828 1566 C ATOM 1187 N MET A 204 220.135 24.681 72.435 1.00 73.53 N ANISOU 1187 N MET A 204 11617 6981 9342 -1387 -1339 1496 N ATOM 1188 CA MET A 204 219.651 23.480 71.764 1.00 75.63 C ANISOU 1188 CA MET A 204 11636 7453 9646 -1338 -1124 1441 C ATOM 1189 C MET A 204 218.468 23.760 70.847 1.00 79.37 C ANISOU 1189 C MET A 204 12210 7806 10140 -1257 -1296 1449 C ATOM 1190 O MET A 204 218.229 22.988 69.912 1.00 81.90 O ANISOU 1190 O MET A 204 12393 8287 10437 -1326 -1174 1456 O ATOM 1191 CB MET A 204 219.274 22.414 72.792 1.00 77.79 C ANISOU 1191 CB MET A 204 11648 7839 10068 -1060 -877 1289 C ATOM 1192 CG MET A 204 220.450 21.937 73.622 1.00 77.21 C ANISOU 1192 CG MET A 204 11451 7905 9981 -1134 -695 1273 C ATOM 1193 SD MET A 204 221.775 21.258 72.603 1.00 68.93 S ANISOU 1193 SD MET A 204 10268 7143 8781 -1478 -540 1338 S ATOM 1194 CE MET A 204 221.122 19.637 72.224 1.00 66.57 C ANISOU 1194 CE MET A 204 9681 7031 8581 -1320 -303 1226 C ATOM 1195 N LEU A 205 217.725 24.843 71.088 1.00 80.90 N ANISOU 1195 N LEU A 205 12641 7721 10378 -1098 -1591 1434 N ATOM 1196 CA LEU A 205 216.632 25.204 70.194 1.00 83.59 C ANISOU 1196 CA LEU A 205 13100 7927 10732 -1015 -1801 1435 C ATOM 1197 C LEU A 205 217.133 25.699 68.845 1.00 87.99 C ANISOU 1197 C LEU A 205 13865 8453 11113 -1387 -1969 1627 C ATOM 1198 O LEU A 205 216.369 25.693 67.874 1.00 93.67 O ANISOU 1198 O LEU A 205 14632 9137 11822 -1384 -2075 1648 O ATOM 1199 CB LEU A 205 215.745 26.267 70.844 1.00 78.65 C ANISOU 1199 CB LEU A 205 12676 7006 10200 -720 -2112 1334 C ATOM 1200 CG LEU A 205 214.968 25.842 72.092 1.00 75.81 C ANISOU 1200 CG LEU A 205 12100 6707 9998 -335 -1977 1111 C ATOM 1201 CD1 LEU A 205 214.252 27.034 72.708 1.00 76.84 C ANISOU 1201 CD1 LEU A 205 12438 6562 10197 -60 -2321 989 C ATOM 1202 CD2 LEU A 205 213.980 24.737 71.754 1.00 71.39 C ANISOU 1202 CD2 LEU A 205 11265 6352 9508 -177 -1766 1002 C ATOM 1203 N PHE A 206 218.392 26.127 68.763 1.00 87.99 N ANISOU 1203 N PHE A 206 13986 8488 10960 -1727 -1996 1765 N ATOM 1204 CA PHE A 206 218.989 26.572 67.512 1.00 88.45 C ANISOU 1204 CA PHE A 206 14226 8577 10805 -2152 -2138 1954 C ATOM 1205 C PHE A 206 220.006 25.598 66.940 1.00 88.35 C ANISOU 1205 C PHE A 206 13952 8955 10662 -2448 -1825 1984 C ATOM 1206 O PHE A 206 220.161 25.537 65.718 1.00 94.09 O ANISOU 1206 O PHE A 206 14705 9808 11235 -2739 -1854 2085 O ATOM 1207 CB PHE A 206 219.665 27.937 67.700 1.00 91.77 C ANISOU 1207 CB PHE A 206 15017 8757 11093 -2389 -2463 2098 C ATOM 1208 CG PHE A 206 218.716 29.038 68.081 1.00 93.17 C ANISOU 1208 CG PHE A 206 15508 8519 11375 -2124 -2854 2067 C ATOM 1209 CD1 PHE A 206 218.014 29.731 67.108 1.00 99.56 C ANISOU 1209 CD1 PHE A 206 16598 9098 12131 -2184 -3199 2154 C ATOM 1210 CD2 PHE A 206 218.525 29.379 69.409 1.00 90.18 C ANISOU 1210 CD2 PHE A 206 15139 7983 11142 -1806 -2896 1934 C ATOM 1211 CE1 PHE A 206 217.140 30.746 67.452 1.00103.25 C ANISOU 1211 CE1 PHE A 206 17354 9174 12700 -1906 -3597 2094 C ATOM 1212 CE2 PHE A 206 217.652 30.392 69.760 1.00 93.34 C ANISOU 1212 CE2 PHE A 206 15808 8018 11638 -1534 -3274 1864 C ATOM 1213 CZ PHE A 206 216.959 31.077 68.781 1.00 99.56 C ANISOU 1213 CZ PHE A 206 16877 8567 12382 -1570 -3635 1936 C ATOM 1214 N THR A 207 220.696 24.835 67.789 1.00 82.13 N ANISOU 1214 N THR A 207 12909 8369 9929 -2375 -1542 1886 N ATOM 1215 CA THR A 207 221.698 23.896 67.295 1.00 81.61 C ANISOU 1215 CA THR A 207 12579 8683 9747 -2615 -1268 1871 C ATOM 1216 C THR A 207 221.046 22.716 66.586 1.00 83.66 C ANISOU 1216 C THR A 207 12585 9124 10077 -2493 -1070 1781 C ATOM 1217 O THR A 207 221.480 22.314 65.500 1.00 89.88 O ANISOU 1217 O THR A 207 13273 10159 10720 -2759 -992 1814 O ATOM 1218 CB THR A 207 222.575 23.408 68.447 1.00 82.05 C ANISOU 1218 CB THR A 207 12449 8870 9857 -2531 -1058 1774 C ATOM 1219 OG1 THR A 207 223.185 24.531 69.095 1.00 85.43 O ANISOU 1219 OG1 THR A 207 13117 9129 10212 -2654 -1246 1861 O ATOM 1220 CG2 THR A 207 223.659 22.477 67.930 1.00 79.47 C ANISOU 1220 CG2 THR A 207 11846 8943 9407 -2757 -812 1724 C ATOM 1221 N MET A 208 220.004 22.148 67.184 1.00 79.38 N ANISOU 1221 N MET A 208 11933 8484 9745 -2109 -990 1660 N ATOM 1222 CA MET A 208 219.328 20.985 66.630 1.00 75.12 C ANISOU 1222 CA MET A 208 11160 8100 9282 -1977 -805 1571 C ATOM 1223 C MET A 208 218.158 21.404 65.746 1.00 74.75 C ANISOU 1223 C MET A 208 11259 7899 9244 -1932 -993 1620 C ATOM 1224 O MET A 208 217.637 22.518 65.841 1.00 79.95 O ANISOU 1224 O MET A 208 12187 8283 9908 -1883 -1274 1681 O ATOM 1225 CB MET A 208 218.831 20.069 67.747 1.00 72.49 C ANISOU 1225 CB MET A 208 10624 7774 9143 -1629 -614 1418 C ATOM 1226 CG MET A 208 219.862 19.794 68.820 1.00 74.22 C ANISOU 1226 CG MET A 208 10747 8076 9378 -1623 -479 1369 C ATOM 1227 SD MET A 208 221.241 18.814 68.205 1.00 72.30 S ANISOU 1227 SD MET A 208 10265 8196 9011 -1875 -263 1332 S ATOM 1228 CE MET A 208 220.415 17.279 67.796 1.00 73.30 C ANISOU 1228 CE MET A 208 10139 8451 9259 -1673 -70 1209 C ATOM 1229 N GLY A 209 217.745 20.482 64.881 1.00 73.61 N ANISOU 1229 N GLY A 209 10936 7929 9105 -1935 -852 1581 N ATOM 1230 CA GLY A 209 216.639 20.729 63.979 1.00 75.57 C ANISOU 1230 CA GLY A 209 11287 8067 9361 -1891 -1005 1616 C ATOM 1231 C GLY A 209 216.438 19.607 62.982 1.00 76.85 C ANISOU 1231 C GLY A 209 11223 8474 9502 -1949 -812 1576 C ATOM 1232 O GLY A 209 217.330 18.777 62.784 1.00 74.99 O ANISOU 1232 O GLY A 209 10783 8505 9206 -2091 -600 1534 O ATOM 1233 N LEU A 210 215.269 19.569 62.351 1.00 77.66 N ANISOU 1233 N LEU A 210 11356 8494 9656 -1828 -897 1569 N ATOM 1234 CA LEU A 210 214.978 18.526 61.379 1.00 74.34 C ANISOU 1234 CA LEU A 210 10734 8290 9221 -1873 -728 1529 C ATOM 1235 C LEU A 210 215.753 18.771 60.088 1.00 73.70 C ANISOU 1235 C LEU A 210 10708 8372 8922 -2276 -778 1647 C ATOM 1236 O LEU A 210 215.986 19.913 59.681 1.00 74.99 O ANISOU 1236 O LEU A 210 11139 8403 8951 -2502 -1027 1792 O ATOM 1237 CB LEU A 210 213.476 18.469 61.097 1.00 68.79 C ANISOU 1237 CB LEU A 210 10049 7460 8628 -1631 -813 1485 C ATOM 1238 CG LEU A 210 212.952 17.270 60.304 1.00 64.78 C ANISOU 1238 CG LEU A 210 9315 7152 8146 -1603 -623 1418 C ATOM 1239 CD1 LEU A 210 213.129 15.984 61.094 1.00 64.32 C ANISOU 1239 CD1 LEU A 210 8992 7251 8197 -1443 -343 1283 C ATOM 1240 CD2 LEU A 210 211.495 17.478 59.921 1.00 65.59 C ANISOU 1240 CD2 LEU A 210 9479 7120 8322 -1407 -760 1394 C ATOM 1241 N GLN A 211 216.158 17.680 59.442 1.00 74.67 N ANISOU 1241 N GLN A 211 10579 8793 8998 -2378 -553 1578 N ATOM 1242 CA GLN A 211 216.960 17.765 58.230 1.00 79.63 C ANISOU 1242 CA GLN A 211 11194 9662 9399 -2773 -558 1651 C ATOM 1243 C GLN A 211 216.761 16.493 57.417 1.00 82.38 C ANISOU 1243 C GLN A 211 11269 10272 9759 -2751 -348 1538 C ATOM 1244 O GLN A 211 216.688 15.398 57.982 1.00 81.68 O ANISOU 1244 O GLN A 211 10957 10262 9817 -2510 -146 1389 O ATOM 1245 CB GLN A 211 218.442 17.970 58.569 1.00 86.58 C ANISOU 1245 CB GLN A 211 12033 10728 10136 -3019 -499 1654 C ATOM 1246 CG GLN A 211 219.339 18.251 57.379 1.00 92.71 C ANISOU 1246 CG GLN A 211 12808 11791 10628 -3485 -529 1730 C ATOM 1247 CD GLN A 211 220.791 18.424 57.781 1.00 97.35 C ANISOU 1247 CD GLN A 211 13319 12602 11065 -3720 -459 1704 C ATOM 1248 OE1 GLN A 211 221.399 17.520 58.354 1.00 97.91 O ANISOU 1248 OE1 GLN A 211 13127 12863 11212 -3575 -244 1533 O ATOM 1249 NE2 GLN A 211 221.355 19.589 57.483 1.00103.13 N ANISOU 1249 NE2 GLN A 211 14295 13313 11578 -4092 -661 1872 N ATOM 1250 N ASN A 212 216.673 16.645 56.094 1.00 83.03 N ANISOU 1250 N ASN A 212 11385 10481 9682 -3013 -415 1613 N ATOM 1251 CA ASN A 212 216.444 15.524 55.185 1.00 81.52 C ANISOU 1251 CA ASN A 212 10952 10537 9484 -3014 -243 1510 C ATOM 1252 C ASN A 212 217.764 15.170 54.511 1.00 75.96 C ANISOU 1252 C ASN A 212 10059 10235 8566 -3345 -119 1449 C ATOM 1253 O ASN A 212 218.261 15.925 53.668 1.00 76.78 O ANISOU 1253 O ASN A 212 10279 10464 8431 -3730 -240 1568 O ATOM 1254 CB ASN A 212 215.378 15.868 54.147 1.00 81.56 C ANISOU 1254 CB ASN A 212 11097 10437 9457 -3066 -394 1612 C ATOM 1255 CG ASN A 212 214.853 14.641 53.417 1.00 80.43 C ANISOU 1255 CG ASN A 212 10709 10481 9368 -2967 -215 1492 C ATOM 1256 OD1 ASN A 212 215.583 13.675 53.191 1.00 81.92 O ANISOU 1256 OD1 ASN A 212 10640 10968 9519 -3020 -13 1355 O ATOM 1257 ND2 ASN A 212 213.580 14.678 53.042 1.00 76.90 N ANISOU 1257 ND2 ASN A 212 10344 9864 9011 -2813 -304 1529 N ATOM 1258 N ARG A 213 218.320 14.012 54.870 1.00 72.02 N ANISOU 1258 N ARG A 213 9271 9952 8142 -3201 104 1251 N ATOM 1259 CA ARG A 213 219.609 13.567 54.357 1.00 69.24 C ANISOU 1259 CA ARG A 213 8685 10018 7603 -3450 229 1126 C ATOM 1260 C ARG A 213 219.490 12.374 53.415 1.00 66.45 C ANISOU 1260 C ARG A 213 8063 9944 7242 -3422 379 959 C ATOM 1261 O ARG A 213 220.468 11.644 53.221 1.00 68.00 O ANISOU 1261 O ARG A 213 7993 10487 7359 -3481 513 765 O ATOM 1262 CB ARG A 213 220.551 13.233 55.513 1.00 71.80 C ANISOU 1262 CB ARG A 213 8886 10395 7999 -3313 331 996 C ATOM 1263 CG ARG A 213 220.967 14.432 56.345 1.00 74.28 C ANISOU 1263 CG ARG A 213 9434 10519 8268 -3414 195 1142 C ATOM 1264 CD ARG A 213 222.161 14.091 57.223 1.00 79.04 C ANISOU 1264 CD ARG A 213 9871 11288 8872 -3373 307 999 C ATOM 1265 NE ARG A 213 222.552 15.204 58.082 1.00 81.78 N ANISOU 1265 NE ARG A 213 10441 11445 9186 -3457 182 1134 N ATOM 1266 CZ ARG A 213 223.592 15.175 58.909 1.00 84.82 C ANISOU 1266 CZ ARG A 213 10736 11938 9553 -3456 243 1049 C ATOM 1267 NH1 ARG A 213 224.344 14.086 58.990 1.00 83.60 N ANISOU 1267 NH1 ARG A 213 10273 12075 9416 -3360 414 817 N ATOM 1268 NH2 ARG A 213 223.880 16.233 59.654 1.00 87.46 N ANISOU 1268 NH2 ARG A 213 11293 12082 9856 -3540 117 1183 N ATOM 1269 N SER A 214 218.321 12.161 52.820 1.00 63.55 N ANISOU 1269 N SER A 214 7752 9442 6953 -3323 346 1013 N ATOM 1270 CA SER A 214 218.160 11.059 51.884 1.00 67.48 C ANISOU 1270 CA SER A 214 8011 10189 7440 -3303 474 861 C ATOM 1271 C SER A 214 218.891 11.353 50.579 1.00 77.27 C ANISOU 1271 C SER A 214 9165 11815 8379 -3732 466 862 C ATOM 1272 O SER A 214 219.046 12.508 50.174 1.00 84.46 O ANISOU 1272 O SER A 214 10283 12709 9097 -4058 314 1052 O ATOM 1273 CB SER A 214 216.681 10.804 51.607 1.00 67.32 C ANISOU 1273 CB SER A 214 8080 9925 7573 -3098 438 927 C ATOM 1274 OG SER A 214 216.518 9.711 50.721 1.00 70.24 O ANISOU 1274 OG SER A 214 8227 10525 7937 -3075 558 779 O ATOM 1275 N ALA A 215 219.349 10.285 49.919 1.00 80.96 N ANISOU 1275 N ALA A 215 9327 12641 8794 -3740 615 638 N ATOM 1276 CA ALA A 215 220.032 10.447 48.638 1.00 85.13 C ANISOU 1276 CA ALA A 215 9721 13607 9018 -4151 629 598 C ATOM 1277 C ALA A 215 219.093 11.037 47.595 1.00 88.32 C ANISOU 1277 C ALA A 215 10320 13914 9324 -4357 506 804 C ATOM 1278 O ALA A 215 219.463 11.957 46.857 1.00 84.06 O ANISOU 1278 O ALA A 215 9898 13530 8512 -4786 396 950 O ATOM 1279 CB ALA A 215 220.595 9.106 48.166 1.00 87.61 C ANISOU 1279 CB ALA A 215 9652 14313 9324 -4053 801 275 C ATOM 1280 N ASP A 216 217.873 10.512 47.516 1.00 93.66 N ANISOU 1280 N ASP A 216 11038 14340 10209 -4071 511 821 N ATOM 1281 CA ASP A 216 216.824 11.168 46.751 1.00 97.14 C ANISOU 1281 CA ASP A 216 11711 14591 10606 -4191 359 1033 C ATOM 1282 C ASP A 216 216.640 12.595 47.256 1.00101.19 C ANISOU 1282 C ASP A 216 12586 14774 11085 -4305 132 1288 C ATOM 1283 O ASP A 216 216.803 12.879 48.447 1.00103.61 O ANISOU 1283 O ASP A 216 12981 14859 11526 -4114 111 1301 O ATOM 1284 CB ASP A 216 215.513 10.386 46.877 1.00 98.54 C ANISOU 1284 CB ASP A 216 11875 14518 11046 -3807 401 996 C ATOM 1285 CG ASP A 216 214.486 10.781 45.830 1.00100.87 C ANISOU 1285 CG ASP A 216 12321 14724 11279 -3928 278 1148 C ATOM 1286 OD1 ASP A 216 214.705 11.785 45.119 1.00112.58 O ANISOU 1286 OD1 ASP A 216 13982 16260 12535 -4297 120 1318 O ATOM 1287 OD2 ASP A 216 213.455 10.081 45.720 1.00 95.60 O ANISOU 1287 OD2 ASP A 216 11606 13934 10784 -3667 326 1100 O ATOM 1288 N GLY A 217 216.323 13.503 46.333 1.00103.95 N ANISOU 1288 N GLY A 217 13159 15090 11246 -4627 -58 1489 N ATOM 1289 CA GLY A 217 216.069 14.880 46.728 1.00104.69 C ANISOU 1289 CA GLY A 217 13638 14830 11309 -4727 -329 1730 C ATOM 1290 C GLY A 217 215.028 14.989 47.822 1.00103.60 C ANISOU 1290 C GLY A 217 13648 14235 11482 -4263 -400 1751 C ATOM 1291 O GLY A 217 215.216 15.709 48.805 1.00102.44 O ANISOU 1291 O GLY A 217 13677 13849 11396 -4183 -509 1819 O ATOM 1292 N THR A 218 213.928 14.259 47.678 1.00104.63 N ANISOU 1292 N THR A 218 13691 14264 11799 -3959 -333 1679 N ATOM 1293 CA THR A 218 212.870 14.226 48.676 1.00101.91 C ANISOU 1293 CA THR A 218 13429 13561 11731 -3523 -371 1661 C ATOM 1294 C THR A 218 212.532 12.783 49.031 1.00 96.27 C ANISOU 1294 C THR A 218 12417 12950 11210 -3203 -113 1455 C ATOM 1295 O THR A 218 212.510 11.900 48.166 1.00 98.93 O ANISOU 1295 O THR A 218 12554 13533 11503 -3263 22 1361 O ATOM 1296 CB THR A 218 211.610 14.948 48.205 1.00101.88 C ANISOU 1296 CB THR A 218 13677 13272 11761 -3462 -617 1797 C ATOM 1297 OG1 THR A 218 210.559 14.756 49.165 1.00104.75 O ANISOU 1297 OG1 THR A 218 14047 13371 12383 -3023 -617 1724 O ATOM 1298 CG2 THR A 218 211.152 14.428 46.843 1.00102.81 C ANISOU 1298 CG2 THR A 218 13697 13581 11785 -3606 -578 1796 C ATOM 1299 N HIS A 219 212.275 12.558 50.313 1.00 89.59 N ANISOU 1299 N HIS A 219 11557 11914 10568 -2878 -61 1387 N ATOM 1300 CA HIS A 219 211.831 11.266 50.816 1.00 86.51 C ANISOU 1300 CA HIS A 219 10948 11556 10368 -2572 138 1220 C ATOM 1301 C HIS A 219 211.337 11.477 52.235 1.00 90.15 C ANISOU 1301 C HIS A 219 11493 11745 11014 -2270 109 1211 C ATOM 1302 O HIS A 219 211.630 12.512 52.852 1.00 98.66 O ANISOU 1302 O HIS A 219 12756 12660 12071 -2301 -31 1301 O ATOM 1303 CB HIS A 219 212.968 10.238 50.795 1.00 78.18 C ANISOU 1303 CB HIS A 219 9631 10800 9272 -2633 340 1055 C ATOM 1304 CG HIS A 219 212.487 8.820 50.771 1.00 72.86 C ANISOU 1304 CG HIS A 219 8748 10198 8736 -2410 502 894 C ATOM 1305 ND1 HIS A 219 212.260 8.096 51.917 1.00 67.44 N ANISOU 1305 ND1 HIS A 219 8004 9382 8237 -2123 585 802 N ATOM 1306 CD2 HIS A 219 212.195 7.988 49.740 1.00 73.61 C ANISOU 1306 CD2 HIS A 219 8694 10474 8800 -2449 579 814 C ATOM 1307 CE1 HIS A 219 211.818 6.892 51.599 1.00 67.49 C ANISOU 1307 CE1 HIS A 219 7855 9466 8320 -2002 691 683 C ATOM 1308 NE2 HIS A 219 211.778 6.796 50.283 1.00 70.67 N ANISOU 1308 NE2 HIS A 219 8194 10057 8601 -2183 694 680 N ATOM 1309 N PRO A 220 210.548 10.552 52.772 1.00 83.67 N ANISOU 1309 N PRO A 220 10552 10875 10363 -1991 223 1106 N ATOM 1310 CA PRO A 220 210.203 10.662 54.194 1.00 79.19 C ANISOU 1310 CA PRO A 220 10031 10111 9946 -1736 220 1078 C ATOM 1311 C PRO A 220 211.196 9.951 55.101 1.00 76.14 C ANISOU 1311 C PRO A 220 9517 9807 9608 -1686 368 978 C ATOM 1312 O PRO A 220 211.419 10.377 56.238 1.00 81.92 O ANISOU 1312 O PRO A 220 10322 10404 10399 -1584 340 987 O ATOM 1313 CB PRO A 220 208.811 10.024 54.272 1.00 79.02 C ANISOU 1313 CB PRO A 220 9945 10029 10048 -1507 260 1019 C ATOM 1314 CG PRO A 220 208.784 9.065 53.148 1.00 80.67 C ANISOU 1314 CG PRO A 220 10003 10437 10210 -1608 368 969 C ATOM 1315 CD PRO A 220 209.619 9.658 52.054 1.00 82.25 C ANISOU 1315 CD PRO A 220 10253 10768 10232 -1909 300 1047 C ATOM 1316 N GLY A 221 211.804 8.873 54.610 1.00 67.56 N ANISOU 1316 N GLY A 221 8239 8937 8495 -1748 510 869 N ATOM 1317 CA GLY A 221 212.736 8.091 55.405 1.00 66.34 C ANISOU 1317 CA GLY A 221 7959 8857 8392 -1677 624 749 C ATOM 1318 C GLY A 221 214.114 8.694 55.570 1.00 66.51 C ANISOU 1318 C GLY A 221 7989 8982 8298 -1852 604 755 C ATOM 1319 O GLY A 221 215.004 8.024 56.103 1.00 66.18 O ANISOU 1319 O GLY A 221 7822 9039 8285 -1802 689 632 O ATOM 1320 N GLY A 222 214.317 9.933 55.126 1.00 70.81 N ANISOU 1320 N GLY A 222 8687 9510 8708 -2064 478 891 N ATOM 1321 CA GLY A 222 215.602 10.587 55.261 1.00 72.86 C ANISOU 1321 CA GLY A 222 8969 9884 8830 -2276 449 913 C ATOM 1322 C GLY A 222 215.583 11.716 56.271 1.00 72.60 C ANISOU 1322 C GLY A 222 9156 9599 8829 -2235 320 1033 C ATOM 1323 O GLY A 222 216.624 12.303 56.575 1.00 74.29 O ANISOU 1323 O GLY A 222 9410 9875 8941 -2397 290 1060 O ATOM 1324 N LEU A 223 214.402 12.032 56.795 1.00 69.75 N ANISOU 1324 N LEU A 223 8929 8972 8603 -2020 240 1090 N ATOM 1325 CA LEU A 223 214.275 13.088 57.792 1.00 66.71 C ANISOU 1325 CA LEU A 223 8745 8339 8262 -1938 102 1174 C ATOM 1326 C LEU A 223 214.920 12.645 59.100 1.00 65.32 C ANISOU 1326 C LEU A 223 8483 8154 8181 -1792 213 1085 C ATOM 1327 O LEU A 223 214.515 11.637 59.687 1.00 69.31 O ANISOU 1327 O LEU A 223 8858 8655 8820 -1577 337 981 O ATOM 1328 CB LEU A 223 212.804 13.432 58.009 1.00 66.30 C ANISOU 1328 CB LEU A 223 8807 8057 8327 -1713 -8 1202 C ATOM 1329 CG LEU A 223 212.068 14.013 56.803 1.00 66.23 C ANISOU 1329 CG LEU A 223 8923 8004 8237 -1827 -167 1297 C ATOM 1330 CD1 LEU A 223 210.578 14.113 57.084 1.00 66.46 C ANISOU 1330 CD1 LEU A 223 8998 7855 8399 -1549 -248 1266 C ATOM 1331 CD2 LEU A 223 212.644 15.369 56.445 1.00 70.02 C ANISOU 1331 CD2 LEU A 223 9652 8389 8564 -2079 -393 1448 C ATOM 1332 N VAL A 224 215.920 13.394 59.562 1.00 63.27 N ANISOU 1332 N VAL A 224 8310 7888 7842 -1925 157 1132 N ATOM 1333 CA VAL A 224 216.634 13.047 60.783 1.00 62.75 C ANISOU 1333 CA VAL A 224 8172 7819 7852 -1807 249 1053 C ATOM 1334 C VAL A 224 216.678 14.252 61.712 1.00 63.14 C ANISOU 1334 C VAL A 224 8433 7643 7913 -1779 104 1146 C ATOM 1335 O VAL A 224 216.602 15.406 61.276 1.00 63.26 O ANISOU 1335 O VAL A 224 8654 7553 7830 -1933 -80 1272 O ATOM 1336 CB VAL A 224 218.062 12.536 60.491 1.00 62.96 C ANISOU 1336 CB VAL A 224 8026 8129 7766 -1988 358 964 C ATOM 1337 CG1 VAL A 224 218.009 11.274 59.643 1.00 63.06 C ANISOU 1337 CG1 VAL A 224 7817 8358 7783 -1971 487 834 C ATOM 1338 CG2 VAL A 224 218.886 13.615 59.809 1.00 68.89 C ANISOU 1338 CG2 VAL A 224 8885 8989 8300 -2332 249 1071 C ATOM 1339 N CYS A 225 216.796 13.968 63.009 1.00 65.28 N ANISOU 1339 N CYS A 225 8669 7833 8303 -1584 169 1081 N ATOM 1340 CA CYS A 225 216.910 14.986 64.051 1.00 71.72 C ANISOU 1340 CA CYS A 225 9656 8451 9143 -1527 53 1138 C ATOM 1341 C CYS A 225 218.388 15.100 64.410 1.00 73.06 C ANISOU 1341 C CYS A 225 9790 8745 9224 -1692 98 1130 C ATOM 1342 O CYS A 225 218.900 14.338 65.234 1.00 73.31 O ANISOU 1342 O CYS A 225 9687 8840 9328 -1580 228 1032 O ATOM 1343 CB CYS A 225 216.053 14.620 65.258 1.00 76.36 C ANISOU 1343 CB CYS A 225 10215 8900 9898 -1225 98 1065 C ATOM 1344 SG CYS A 225 216.089 15.798 66.634 1.00 77.90 S ANISOU 1344 SG CYS A 225 10593 8868 10136 -1112 -39 1096 S ATOM 1345 N THR A 226 219.067 16.055 63.789 1.00 72.32 N ANISOU 1345 N THR A 226 9825 8692 8962 -1974 -22 1234 N ATOM 1346 CA THR A 226 220.512 16.196 63.860 1.00 68.87 C ANISOU 1346 CA THR A 226 9332 8446 8388 -2200 20 1224 C ATOM 1347 C THR A 226 220.848 17.673 64.000 1.00 70.03 C ANISOU 1347 C THR A 226 9749 8441 8418 -2397 -188 1376 C ATOM 1348 O THR A 226 220.006 18.533 63.717 1.00 71.53 O ANISOU 1348 O THR A 226 10167 8403 8609 -2394 -384 1488 O ATOM 1349 CB THR A 226 221.176 15.606 62.605 1.00 64.77 C ANISOU 1349 CB THR A 226 8631 8268 7713 -2444 113 1169 C ATOM 1350 OG1 THR A 226 222.555 15.313 62.862 1.00 62.41 O ANISOU 1350 OG1 THR A 226 8170 8222 7319 -2569 212 1070 O ATOM 1351 CG2 THR A 226 221.073 16.575 61.434 1.00 67.61 C ANISOU 1351 CG2 THR A 226 9165 8644 7879 -2764 -51 1322 C ATOM 1352 N PRO A 227 222.053 18.000 64.469 1.00 69.47 N ANISOU 1352 N PRO A 227 9671 8476 8248 -2559 -173 1377 N ATOM 1353 CA PRO A 227 222.472 19.408 64.489 1.00 69.44 C ANISOU 1353 CA PRO A 227 9942 8344 8099 -2809 -388 1535 C ATOM 1354 C PRO A 227 222.444 20.014 63.093 1.00 68.10 C ANISOU 1354 C PRO A 227 9906 8250 7719 -3160 -534 1667 C ATOM 1355 O PRO A 227 222.974 19.442 62.137 1.00 69.34 O ANISOU 1355 O PRO A 227 9878 8737 7733 -3380 -418 1620 O ATOM 1356 CB PRO A 227 223.895 19.344 65.050 1.00 67.11 C ANISOU 1356 CB PRO A 227 9530 8262 7707 -2957 -288 1479 C ATOM 1357 CG PRO A 227 223.895 18.138 65.908 1.00 67.31 C ANISOU 1357 CG PRO A 227 9311 8341 7923 -2631 -81 1303 C ATOM 1358 CD PRO A 227 222.984 17.147 65.232 1.00 67.59 C ANISOU 1358 CD PRO A 227 9205 8421 8055 -2470 12 1230 C ATOM 1359 N ILE A 228 221.819 21.182 62.985 1.00 67.72 N ANISOU 1359 N ILE A 228 10188 7894 7648 -3210 -809 1823 N ATOM 1360 CA ILE A 228 221.649 21.861 61.708 1.00 68.94 C ANISOU 1360 CA ILE A 228 10537 8048 7608 -3541 -1006 1976 C ATOM 1361 C ILE A 228 222.643 23.012 61.547 1.00 77.84 C ANISOU 1361 C ILE A 228 11906 9187 8484 -3975 -1201 2138 C ATOM 1362 O ILE A 228 222.431 23.899 60.723 1.00 84.27 O ANISOU 1362 O ILE A 228 13001 9880 9137 -4255 -1462 2310 O ATOM 1363 CB ILE A 228 220.204 22.345 61.517 1.00 64.30 C ANISOU 1363 CB ILE A 228 10174 7105 7152 -3316 -1227 2037 C ATOM 1364 CG1 ILE A 228 219.813 23.311 62.639 1.00 64.79 C ANISOU 1364 CG1 ILE A 228 10494 6784 7340 -3091 -1445 2067 C ATOM 1365 CG2 ILE A 228 219.249 21.162 61.443 1.00 62.99 C ANISOU 1365 CG2 ILE A 228 9754 6999 7180 -2975 -1025 1889 C ATOM 1366 CD1 ILE A 228 218.435 23.912 62.475 1.00 64.44 C ANISOU 1366 CD1 ILE A 228 10676 6397 7412 -2857 -1709 2094 C ATOM 1367 N VAL A 229 223.724 23.011 62.321 1.00 82.22 N ANISOU 1367 N VAL A 229 12367 9883 8990 -4050 -1095 2090 N ATOM 1368 CA VAL A 229 224.763 24.024 62.221 1.00 88.33 C ANISOU 1368 CA VAL A 229 13339 10717 9504 -4490 -1254 2232 C ATOM 1369 C VAL A 229 226.089 23.329 61.924 1.00 92.29 C ANISOU 1369 C VAL A 229 13510 11742 9814 -4764 -1001 2118 C ATOM 1370 O VAL A 229 226.210 22.106 62.011 1.00 93.55 O ANISOU 1370 O VAL A 229 13313 12147 10085 -4544 -728 1918 O ATOM 1371 CB VAL A 229 224.859 24.891 63.492 1.00 91.50 C ANISOU 1371 CB VAL A 229 13975 10787 10003 -4345 -1412 2281 C ATOM 1372 CG1 VAL A 229 223.608 25.742 63.645 1.00 95.80 C ANISOU 1372 CG1 VAL A 229 14867 10841 10691 -4119 -1722 2377 C ATOM 1373 CG2 VAL A 229 225.045 24.016 64.716 1.00 91.81 C ANISOU 1373 CG2 VAL A 229 13736 10883 10263 -3961 -1150 2088 C ATOM 1374 N ASP A 230 227.088 24.131 61.562 1.00 96.83 N ANISOU 1374 N ASP A 230 14211 12493 10087 -5256 -1115 2238 N ATOM 1375 CA ASP A 230 228.385 23.590 61.188 1.00100.18 C ANISOU 1375 CA ASP A 230 14313 13470 10280 -5565 -901 2114 C ATOM 1376 C ASP A 230 229.090 22.986 62.403 1.00100.57 C ANISOU 1376 C ASP A 230 14114 13623 10477 -5289 -692 1924 C ATOM 1377 O ASP A 230 228.661 23.139 63.550 1.00102.20 O ANISOU 1377 O ASP A 230 14436 13471 10925 -4932 -730 1926 O ATOM 1378 CB ASP A 230 229.247 24.673 60.541 1.00104.64 C ANISOU 1378 CB ASP A 230 15043 14223 10490 -5972 -1113 2184 C ATOM 1379 CG ASP A 230 229.311 25.945 61.367 1.00111.16 C ANISOU 1379 CG ASP A 230 16242 14672 11321 -5979 -1387 2329 C ATOM 1380 OD1 ASP A 230 229.300 25.864 62.612 1.00110.07 O ANISOU 1380 OD1 ASP A 230 16112 14312 11396 -5729 -1321 2312 O ATOM 1381 OD2 ASP A 230 229.368 27.037 60.763 1.00119.12 O ANISOU 1381 OD2 ASP A 230 17541 15606 12114 -6238 -1683 2454 O ATOM 1382 N THR A 231 230.200 22.292 62.133 1.00101.54 N ANISOU 1382 N THR A 231 13880 14262 10437 -5462 -479 1744 N ATOM 1383 CA THR A 231 230.909 21.584 63.196 1.00103.27 C ANISOU 1383 CA THR A 231 13833 14612 10792 -5188 -284 1535 C ATOM 1384 C THR A 231 231.430 22.549 64.253 1.00 99.56 C ANISOU 1384 C THR A 231 13589 13940 10302 -5259 -408 1646 C ATOM 1385 O THR A 231 231.433 22.229 65.449 1.00 96.58 O ANISOU 1385 O THR A 231 13158 13385 10152 -4894 -333 1557 O ATOM 1386 CB THR A 231 232.058 20.762 62.607 1.00105.61 C ANISOU 1386 CB THR A 231 13710 15531 10885 -5385 -77 1299 C ATOM 1387 OG1 THR A 231 231.551 19.888 61.591 1.00110.68 O ANISOU 1387 OG1 THR A 231 14153 16354 11544 -5320 22 1190 O ATOM 1388 CG2 THR A 231 232.723 19.922 63.688 1.00103.37 C ANISOU 1388 CG2 THR A 231 13150 15355 10769 -5047 99 1060 C ATOM 1389 N ALA A 232 231.864 23.741 63.834 1.00101.09 N ANISOU 1389 N ALA A 232 14050 14147 10213 -5743 -611 1849 N ATOM 1390 CA ALA A 232 232.389 24.715 64.786 1.00101.24 C ANISOU 1390 CA ALA A 232 14297 13971 10197 -5794 -758 1938 C ATOM 1391 C ALA A 232 231.325 25.141 65.788 1.00 96.71 C ANISOU 1391 C ALA A 232 14022 12794 9930 -5420 -900 2055 C ATOM 1392 O ALA A 232 231.604 25.261 66.987 1.00 94.82 O ANISOU 1392 O ALA A 232 13798 12405 9825 -5208 -877 2012 O ATOM 1393 CB ALA A 232 232.944 25.929 64.043 1.00104.43 C ANISOU 1393 CB ALA A 232 14941 14479 10260 -6183 -1018 2047 C ATOM 1394 N THR A 233 230.096 25.370 65.319 1.00 96.80 N ANISOU 1394 N THR A 233 14250 12476 10055 -5287 -1056 2163 N ATOM 1395 CA THR A 233 229.020 25.743 66.231 1.00 93.09 C ANISOU 1395 CA THR A 233 14016 11480 9874 -4860 -1198 2207 C ATOM 1396 C THR A 233 228.596 24.561 67.095 1.00 85.76 C ANISOU 1396 C THR A 233 12792 10541 9254 -4332 -944 1995 C ATOM 1397 O THR A 233 228.332 24.726 68.292 1.00 85.76 O ANISOU 1397 O THR A 233 12864 10272 9447 -4022 -965 1965 O ATOM 1398 CB THR A 233 227.828 26.295 65.447 1.00 94.36 C ANISOU 1398 CB THR A 233 14468 11325 10058 -4857 -1449 2352 C ATOM 1399 OG1 THR A 233 228.261 27.388 64.625 1.00103.03 O ANISOU 1399 OG1 THR A 233 15813 12467 10865 -5264 -1713 2486 O ATOM 1400 CG2 THR A 233 226.741 26.786 66.396 1.00 91.63 C ANISOU 1400 CG2 THR A 233 14359 10469 9988 -4421 -1625 2365 C ATOM 1401 N VAL A 234 228.530 23.361 66.511 1.00 77.38 N ANISOU 1401 N VAL A 234 11404 9767 8228 -4237 -716 1846 N ATOM 1402 CA VAL A 234 228.248 22.168 67.305 1.00 72.45 C ANISOU 1402 CA VAL A 234 10509 9153 7865 -3788 -490 1650 C ATOM 1403 C VAL A 234 229.332 21.968 68.355 1.00 70.84 C ANISOU 1403 C VAL A 234 10160 9088 7668 -3747 -371 1545 C ATOM 1404 O VAL A 234 229.057 21.547 69.486 1.00 71.27 O ANISOU 1404 O VAL A 234 10164 8970 7945 -3387 -297 1462 O ATOM 1405 CB VAL A 234 228.112 20.932 66.396 1.00 70.72 C ANISOU 1405 CB VAL A 234 9984 9234 7654 -3739 -298 1506 C ATOM 1406 CG1 VAL A 234 227.866 19.678 67.230 1.00 68.73 C ANISOU 1406 CG1 VAL A 234 9486 8972 7658 -3304 -100 1315 C ATOM 1407 CG2 VAL A 234 226.998 21.127 65.390 1.00 74.73 C ANISOU 1407 CG2 VAL A 234 10636 9595 8163 -3766 -415 1613 C ATOM 1408 N LYS A 235 230.581 22.275 67.999 1.00 71.61 N ANISOU 1408 N LYS A 235 10185 9518 7505 -4134 -356 1544 N ATOM 1409 CA LYS A 235 231.684 22.125 68.942 1.00 71.72 C ANISOU 1409 CA LYS A 235 10052 9695 7502 -4119 -253 1435 C ATOM 1410 C LYS A 235 231.483 23.008 70.167 1.00 70.09 C ANISOU 1410 C LYS A 235 10122 9098 7413 -3982 -394 1547 C ATOM 1411 O LYS A 235 231.545 22.533 71.306 1.00 66.01 O ANISOU 1411 O LYS A 235 9506 8490 7085 -3665 -294 1441 O ATOM 1412 CB LYS A 235 233.005 22.455 68.248 1.00 69.23 C ANISOU 1412 CB LYS A 235 9626 9834 6845 -4611 -238 1421 C ATOM 1413 CG LYS A 235 234.216 21.749 68.827 1.00 70.41 C ANISOU 1413 CG LYS A 235 9444 10343 6964 -4563 -53 1197 C ATOM 1414 CD LYS A 235 235.500 22.352 68.285 1.00 71.11 C ANISOU 1414 CD LYS A 235 9467 10867 6685 -5090 -73 1203 C ATOM 1415 CE LYS A 235 235.793 23.696 68.932 1.00 73.74 C ANISOU 1415 CE LYS A 235 10142 10960 6916 -5322 -262 1416 C ATOM 1416 NZ LYS A 235 236.980 24.358 68.325 1.00 76.44 N ANISOU 1416 NZ LYS A 235 10454 11732 6859 -5906 -302 1453 N ATOM 1417 N VAL A 236 231.222 24.299 69.948 1.00 76.52 N ANISOU 1417 N VAL A 236 11295 9667 8112 -4219 -646 1757 N ATOM 1418 CA VAL A 236 231.120 25.240 71.061 1.00 78.37 C ANISOU 1418 CA VAL A 236 11804 9543 8431 -4118 -810 1851 C ATOM 1419 C VAL A 236 229.946 24.881 71.965 1.00 77.54 C ANISOU 1419 C VAL A 236 11721 9092 8648 -3601 -793 1787 C ATOM 1420 O VAL A 236 230.057 24.927 73.197 1.00 83.22 O ANISOU 1420 O VAL A 236 12445 9672 9503 -3375 -764 1735 O ATOM 1421 CB VAL A 236 231.010 26.683 70.531 1.00 79.11 C ANISOU 1421 CB VAL A 236 12309 9415 8334 -4475 -1135 2085 C ATOM 1422 CG1 VAL A 236 230.726 27.654 71.669 1.00 75.79 C ANISOU 1422 CG1 VAL A 236 12192 8571 8032 -4308 -1340 2161 C ATOM 1423 CG2 VAL A 236 232.278 27.073 69.787 1.00 79.64 C ANISOU 1423 CG2 VAL A 236 12353 9863 8043 -5043 -1148 2153 C ATOM 1424 N VAL A 237 228.809 24.507 71.373 1.00 72.22 N ANISOU 1424 N VAL A 237 11049 8303 8088 -3422 -805 1782 N ATOM 1425 CA VAL A 237 227.624 24.207 72.173 1.00 69.83 C ANISOU 1425 CA VAL A 237 10761 7711 8059 -2966 -797 1715 C ATOM 1426 C VAL A 237 227.875 23.004 73.072 1.00 73.06 C ANISOU 1426 C VAL A 237 10867 8266 8625 -2687 -536 1540 C ATOM 1427 O VAL A 237 227.539 23.020 74.263 1.00 75.05 O ANISOU 1427 O VAL A 237 11147 8330 9039 -2412 -528 1493 O ATOM 1428 CB VAL A 237 226.402 23.990 71.262 1.00 68.27 C ANISOU 1428 CB VAL A 237 10598 7415 7926 -2861 -853 1733 C ATOM 1429 CG1 VAL A 237 225.213 23.496 72.075 1.00 62.85 C ANISOU 1429 CG1 VAL A 237 9855 6524 7500 -2406 -800 1628 C ATOM 1430 CG2 VAL A 237 226.052 25.277 70.534 1.00 74.39 C ANISOU 1430 CG2 VAL A 237 11730 7963 8569 -3095 -1170 1912 C ATOM 1431 N ILE A 238 228.484 21.950 72.525 1.00 74.76 N ANISOU 1431 N ILE A 238 10796 8821 8787 -2758 -339 1433 N ATOM 1432 CA ILE A 238 228.731 20.750 73.318 1.00 72.88 C ANISOU 1432 CA ILE A 238 10296 8698 8696 -2494 -132 1264 C ATOM 1433 C ILE A 238 229.728 21.028 74.440 1.00 72.94 C ANISOU 1433 C ILE A 238 10298 8726 8688 -2506 -113 1237 C ATOM 1434 O ILE A 238 229.591 20.490 75.545 1.00 68.02 O ANISOU 1434 O ILE A 238 9604 8009 8230 -2230 -33 1155 O ATOM 1435 CB ILE A 238 229.190 19.598 72.402 1.00 70.03 C ANISOU 1435 CB ILE A 238 9644 8689 8276 -2559 30 1133 C ATOM 1436 CG1 ILE A 238 228.034 19.158 71.499 1.00 68.92 C ANISOU 1436 CG1 ILE A 238 9497 8488 8201 -2467 31 1147 C ATOM 1437 CG2 ILE A 238 229.705 18.419 73.214 1.00 68.52 C ANISOU 1437 CG2 ILE A 238 9207 8620 8206 -2326 193 953 C ATOM 1438 CD1 ILE A 238 228.354 17.983 70.607 1.00 67.20 C ANISOU 1438 CD1 ILE A 238 8998 8588 7945 -2493 178 1003 C ATOM 1439 N GLN A 239 230.721 21.888 74.197 1.00 76.97 N ANISOU 1439 N GLN A 239 10895 9361 8989 -2844 -195 1311 N ATOM 1440 CA GLN A 239 231.718 22.184 75.225 1.00 80.26 C ANISOU 1440 CA GLN A 239 11302 9817 9375 -2878 -178 1284 C ATOM 1441 C GLN A 239 231.097 22.897 76.420 1.00 80.96 C ANISOU 1441 C GLN A 239 11622 9527 9612 -2664 -293 1354 C ATOM 1442 O GLN A 239 231.259 22.461 77.566 1.00 80.79 O ANISOU 1442 O GLN A 239 11514 9462 9722 -2435 -204 1268 O ATOM 1443 CB GLN A 239 232.849 23.026 74.639 1.00 79.78 C ANISOU 1443 CB GLN A 239 11300 9984 9028 -3330 -256 1361 C ATOM 1444 CG GLN A 239 233.664 22.331 73.572 1.00 80.38 C ANISOU 1444 CG GLN A 239 11095 10523 8922 -3564 -127 1247 C ATOM 1445 CD GLN A 239 235.091 22.830 73.530 1.00 82.27 C ANISOU 1445 CD GLN A 239 11270 11088 8901 -3935 -127 1233 C ATOM 1446 OE1 GLN A 239 235.630 23.115 72.461 1.00 84.06 O ANISOU 1446 OE1 GLN A 239 11453 11620 8864 -4329 -149 1260 O ATOM 1447 NE2 GLN A 239 235.714 22.939 74.697 1.00 82.65 N ANISOU 1447 NE2 GLN A 239 11303 11094 9004 -3831 -101 1187 N ATOM 1448 N VAL A 240 230.400 24.010 76.173 1.00 84.04 N ANISOU 1448 N VAL A 240 12311 9645 9975 -2736 -509 1499 N ATOM 1449 CA VAL A 240 229.793 24.763 77.267 1.00 82.56 C ANISOU 1449 CA VAL A 240 12340 9111 9919 -2521 -646 1535 C ATOM 1450 C VAL A 240 228.829 23.880 78.050 1.00 82.56 C ANISOU 1450 C VAL A 240 12202 9011 10157 -2107 -521 1414 C ATOM 1451 O VAL A 240 228.798 23.914 79.286 1.00 82.14 O ANISOU 1451 O VAL A 240 12153 8845 10212 -1909 -498 1363 O ATOM 1452 CB VAL A 240 229.097 26.026 76.727 1.00 77.51 C ANISOU 1452 CB VAL A 240 12045 8186 9220 -2632 -938 1681 C ATOM 1453 CG1 VAL A 240 228.439 26.796 77.860 1.00 69.08 C ANISOU 1453 CG1 VAL A 240 11181 6773 8293 -2371 -1098 1673 C ATOM 1454 CG2 VAL A 240 230.097 26.901 75.992 1.00 80.42 C ANISOU 1454 CG2 VAL A 240 12577 8657 9320 -3102 -1080 1823 C ATOM 1455 N ASN A 241 228.042 23.063 77.346 1.00 84.85 N ANISOU 1455 N ASN A 241 12365 9358 10514 -1994 -438 1368 N ATOM 1456 CA ASN A 241 227.174 22.104 78.021 1.00 85.29 C ANISOU 1456 CA ASN A 241 12276 9368 10765 -1654 -309 1256 C ATOM 1457 C ASN A 241 227.992 21.122 78.851 1.00 85.47 C ANISOU 1457 C ASN A 241 12084 9558 10834 -1575 -123 1152 C ATOM 1458 O ASN A 241 227.693 20.884 80.027 1.00 82.36 O ANISOU 1458 O ASN A 241 11672 9062 10561 -1358 -82 1098 O ATOM 1459 CB ASN A 241 226.313 21.367 76.991 1.00 85.29 C ANISOU 1459 CB ASN A 241 12176 9431 10801 -1599 -254 1232 C ATOM 1460 CG ASN A 241 225.211 20.527 77.627 1.00 86.33 C ANISOU 1460 CG ASN A 241 12201 9491 11110 -1280 -159 1138 C ATOM 1461 OD1 ASN A 241 225.460 19.721 78.524 1.00 90.24 O ANISOU 1461 OD1 ASN A 241 12558 10046 11682 -1150 -27 1057 O ATOM 1462 ND2 ASN A 241 223.983 20.713 77.154 1.00 83.35 N ANISOU 1462 ND2 ASN A 241 11892 8995 10783 -1172 -238 1148 N ATOM 1463 N THR A 242 229.039 20.548 78.252 1.00 89.24 N ANISOU 1463 N THR A 242 12394 10306 11208 -1751 -25 1110 N ATOM 1464 CA THR A 242 229.843 19.549 78.950 1.00 88.61 C ANISOU 1464 CA THR A 242 12108 10385 11176 -1656 119 987 C ATOM 1465 C THR A 242 230.524 20.146 80.174 1.00 85.29 C ANISOU 1465 C THR A 242 11766 9887 10754 -1650 86 1001 C ATOM 1466 O THR A 242 230.467 19.575 81.269 1.00 84.34 O ANISOU 1466 O THR A 242 11586 9705 10753 -1445 150 935 O ATOM 1467 CB THR A 242 230.880 18.944 78.000 1.00 88.27 C ANISOU 1467 CB THR A 242 11860 10677 11003 -1843 199 904 C ATOM 1468 OG1 THR A 242 230.215 18.370 76.867 1.00 94.27 O ANISOU 1468 OG1 THR A 242 12543 11507 11766 -1842 230 885 O ATOM 1469 CG2 THR A 242 231.694 17.871 78.705 1.00 81.97 C ANISOU 1469 CG2 THR A 242 10851 10026 10266 -1704 310 748 C ATOM 1470 N PHE A 243 231.164 21.305 80.014 1.00 82.75 N ANISOU 1470 N PHE A 243 11593 9563 10285 -1894 -26 1093 N ATOM 1471 CA PHE A 243 231.875 21.904 81.139 1.00 78.92 C ANISOU 1471 CA PHE A 243 11185 9014 9786 -1909 -61 1107 C ATOM 1472 C PHE A 243 230.906 22.292 82.250 1.00 71.53 C ANISOU 1472 C PHE A 243 10397 7778 9002 -1657 -124 1127 C ATOM 1473 O PHE A 243 231.121 21.956 83.420 1.00 62.56 O ANISOU 1473 O PHE A 243 9206 6613 7951 -1503 -61 1067 O ATOM 1474 CB PHE A 243 232.687 23.115 80.666 1.00 81.31 C ANISOU 1474 CB PHE A 243 11647 9367 9882 -2257 -192 1217 C ATOM 1475 CG PHE A 243 233.082 24.063 81.773 1.00 83.17 C ANISOU 1475 CG PHE A 243 12057 9436 10110 -2271 -290 1270 C ATOM 1476 CD1 PHE A 243 232.223 25.061 82.216 1.00 84.82 C ANISOU 1476 CD1 PHE A 243 12533 9313 10382 -2177 -466 1355 C ATOM 1477 CD2 PHE A 243 234.319 23.936 82.383 1.00 84.66 C ANISOU 1477 CD2 PHE A 243 12130 9808 10228 -2363 -216 1214 C ATOM 1478 CE1 PHE A 243 232.596 25.913 83.240 1.00 85.28 C ANISOU 1478 CE1 PHE A 243 12747 9221 10435 -2179 -564 1388 C ATOM 1479 CE2 PHE A 243 234.698 24.787 83.404 1.00 86.07 C ANISOU 1479 CE2 PHE A 243 12466 9840 10398 -2380 -302 1263 C ATOM 1480 CZ PHE A 243 233.836 25.776 83.833 1.00 86.13 C ANISOU 1480 CZ PHE A 243 12746 9509 10470 -2291 -475 1352 C ATOM 1481 N MET A 244 229.826 22.995 81.896 1.00 78.66 N ANISOU 1481 N MET A 244 11481 8472 9933 -1611 -260 1195 N ATOM 1482 CA MET A 244 228.901 23.519 82.898 1.00 85.21 C ANISOU 1482 CA MET A 244 12444 9050 10883 -1378 -347 1182 C ATOM 1483 C MET A 244 228.322 22.407 83.761 1.00 86.66 C ANISOU 1483 C MET A 244 12451 9261 11214 -1109 -191 1073 C ATOM 1484 O MET A 244 228.460 22.422 84.988 1.00 93.16 O ANISOU 1484 O MET A 244 13269 10034 12092 -993 -164 1031 O ATOM 1485 CB MET A 244 227.780 24.312 82.223 1.00 89.75 C ANISOU 1485 CB MET A 244 13208 9427 11467 -1342 -530 1234 C ATOM 1486 CG MET A 244 228.180 25.713 81.812 1.00 92.92 C ANISOU 1486 CG MET A 244 13886 9683 11738 -1571 -769 1355 C ATOM 1487 SD MET A 244 229.074 26.539 83.136 1.00 91.44 S ANISOU 1487 SD MET A 244 13819 9399 11523 -1603 -838 1365 S ATOM 1488 CE MET A 244 227.717 27.177 84.115 1.00 94.45 C ANISOU 1488 CE MET A 244 14339 9484 12065 -1245 -992 1277 C ATOM 1489 N SER A 245 227.662 21.430 83.143 1.00 81.18 N ANISOU 1489 N SER A 245 11622 8649 10575 -1028 -96 1031 N ATOM 1490 CA SER A 245 227.065 20.357 83.930 1.00 82.52 C ANISOU 1490 CA SER A 245 11651 8840 10861 -814 30 944 C ATOM 1491 C SER A 245 228.134 19.439 84.510 1.00 88.28 C ANISOU 1491 C SER A 245 12237 9710 11596 -832 150 895 C ATOM 1492 O SER A 245 228.235 19.279 85.728 1.00 93.31 O ANISOU 1492 O SER A 245 12867 10304 12283 -731 179 863 O ATOM 1493 CB SER A 245 226.072 19.562 83.085 1.00 80.88 C ANISOU 1493 CB SER A 245 11353 8676 10700 -742 83 919 C ATOM 1494 OG SER A 245 226.744 18.819 82.090 1.00 82.57 O ANISOU 1494 OG SER A 245 11447 9061 10865 -870 156 914 O ATOM 1495 N PHE A 246 228.950 18.821 83.658 1.00 89.80 N ANISOU 1495 N PHE A 246 12309 10081 11731 -955 207 874 N ATOM 1496 CA PHE A 246 229.866 17.802 84.161 1.00 87.64 C ANISOU 1496 CA PHE A 246 11884 9937 11479 -921 295 790 C ATOM 1497 C PHE A 246 230.927 18.396 85.084 1.00 85.73 C ANISOU 1497 C PHE A 246 11684 9700 11191 -983 270 795 C ATOM 1498 O PHE A 246 231.047 18.001 86.249 1.00 86.46 O ANISOU 1498 O PHE A 246 11761 9740 11351 -862 297 760 O ATOM 1499 CB PHE A 246 230.527 17.052 83.008 1.00 87.31 C ANISOU 1499 CB PHE A 246 11682 10114 11379 -1018 343 723 C ATOM 1500 CG PHE A 246 231.229 15.811 83.446 1.00 84.93 C ANISOU 1500 CG PHE A 246 11222 9920 11129 -916 400 601 C ATOM 1501 CD1 PHE A 246 230.596 14.903 84.279 1.00 83.31 C ANISOU 1501 CD1 PHE A 246 11015 9593 11045 -729 419 576 C ATOM 1502 CD2 PHE A 246 232.541 15.580 83.081 1.00 81.06 C ANISOU 1502 CD2 PHE A 246 10590 9655 10552 -1015 412 503 C ATOM 1503 CE1 PHE A 246 231.246 13.766 84.704 1.00 81.32 C ANISOU 1503 CE1 PHE A 246 10658 9399 10842 -634 424 470 C ATOM 1504 CE2 PHE A 246 233.197 14.450 83.507 1.00 79.39 C ANISOU 1504 CE2 PHE A 246 10243 9524 10398 -887 425 365 C ATOM 1505 CZ PHE A 246 232.550 13.540 84.320 1.00 80.31 C ANISOU 1505 CZ PHE A 246 10394 9471 10649 -692 418 356 C ATOM 1506 N LEU A 247 231.708 19.353 84.582 1.00 84.08 N ANISOU 1506 N LEU A 247 11534 9559 10853 -1192 211 844 N ATOM 1507 CA LEU A 247 232.923 19.745 85.286 1.00 84.03 C ANISOU 1507 CA LEU A 247 11524 9624 10780 -1285 203 830 C ATOM 1508 C LEU A 247 232.658 20.657 86.480 1.00 85.16 C ANISOU 1508 C LEU A 247 11840 9556 10960 -1221 133 890 C ATOM 1509 O LEU A 247 233.390 20.586 87.473 1.00 87.36 O ANISOU 1509 O LEU A 247 12091 9853 11247 -1192 156 856 O ATOM 1510 CB LEU A 247 233.893 20.407 84.311 1.00 79.29 C ANISOU 1510 CB LEU A 247 10916 9215 9996 -1577 165 858 C ATOM 1511 CG LEU A 247 234.321 19.440 83.204 1.00 73.64 C ANISOU 1511 CG LEU A 247 9980 8772 9227 -1638 245 754 C ATOM 1512 CD1 LEU A 247 235.198 20.128 82.166 1.00 78.81 C ANISOU 1512 CD1 LEU A 247 10615 9666 9664 -1972 212 779 C ATOM 1513 CD2 LEU A 247 235.021 18.228 83.801 1.00 68.57 C ANISOU 1513 CD2 LEU A 247 9134 8263 8657 -1476 325 595 C ATOM 1514 N PHE A 248 231.637 21.513 86.413 1.00 86.33 N ANISOU 1514 N PHE A 248 12162 9508 11130 -1185 36 962 N ATOM 1515 CA PHE A 248 231.329 22.386 87.542 1.00 86.84 C ANISOU 1515 CA PHE A 248 12380 9381 11233 -1096 -46 985 C ATOM 1516 C PHE A 248 230.909 21.554 88.760 1.00 81.21 C ANISOU 1516 C PHE A 248 11575 8643 10638 -877 48 910 C ATOM 1517 O PHE A 248 231.626 21.583 89.768 1.00 83.60 O ANISOU 1517 O PHE A 248 11869 8955 10939 -870 68 892 O ATOM 1518 CB PHE A 248 230.284 23.430 87.131 1.00 90.22 C ANISOU 1518 CB PHE A 248 13002 9612 11664 -1072 -201 1039 C ATOM 1519 CG PHE A 248 230.284 24.674 87.963 1.00 95.07 C ANISOU 1519 CG PHE A 248 13816 10038 12267 -1055 -350 1065 C ATOM 1520 CD1 PHE A 248 231.417 25.455 88.090 1.00100.03 C ANISOU 1520 CD1 PHE A 248 14549 10672 12785 -1261 -424 1129 C ATOM 1521 CD2 PHE A 248 229.124 25.067 88.615 1.00 96.85 C ANISOU 1521 CD2 PHE A 248 14115 10098 12585 -831 -426 1006 C ATOM 1522 CE1 PHE A 248 231.395 26.607 88.859 1.00103.91 C ANISOU 1522 CE1 PHE A 248 15243 10969 13270 -1240 -582 1149 C ATOM 1523 CE2 PHE A 248 229.094 26.213 89.383 1.00101.00 C ANISOU 1523 CE2 PHE A 248 14821 10448 13106 -787 -583 1001 C ATOM 1524 CZ PHE A 248 230.231 26.985 89.507 1.00103.99 C ANISOU 1524 CZ PHE A 248 15329 10796 13386 -989 -667 1080 C ATOM 1525 N PRO A 249 229.778 20.788 88.738 1.00 75.55 N ANISOU 1525 N PRO A 249 10792 7906 10009 -718 102 869 N ATOM 1526 CA PRO A 249 229.577 19.792 89.801 1.00 75.22 C ANISOU 1526 CA PRO A 249 10652 7887 10040 -582 193 811 C ATOM 1527 C PRO A 249 230.772 18.908 90.132 1.00 73.15 C ANISOU 1527 C PRO A 249 10280 7741 9772 -622 257 779 C ATOM 1528 O PRO A 249 231.159 18.884 91.303 1.00 72.88 O ANISOU 1528 O PRO A 249 10259 7680 9753 -581 264 764 O ATOM 1529 CB PRO A 249 228.393 18.973 89.276 1.00 76.08 C ANISOU 1529 CB PRO A 249 10691 8011 10204 -489 240 785 C ATOM 1530 CG PRO A 249 227.582 19.961 88.548 1.00 73.73 C ANISOU 1530 CG PRO A 249 10496 7628 9890 -487 148 811 C ATOM 1531 CD PRO A 249 228.501 21.038 88.038 1.00 72.62 C ANISOU 1531 CD PRO A 249 10471 7456 9666 -649 51 876 C ATOM 1532 N MET A 250 231.372 18.197 89.167 1.00 72.42 N ANISOU 1532 N MET A 250 10076 7783 9656 -689 292 750 N ATOM 1533 CA MET A 250 232.463 17.282 89.514 1.00 74.03 C ANISOU 1533 CA MET A 250 10163 8101 9866 -680 324 678 C ATOM 1534 C MET A 250 233.512 17.962 90.383 1.00 76.76 C ANISOU 1534 C MET A 250 10547 8457 10163 -741 298 682 C ATOM 1535 O MET A 250 233.995 17.376 91.360 1.00 78.06 O ANISOU 1535 O MET A 250 10677 8618 10365 -666 305 639 O ATOM 1536 CB MET A 250 233.133 16.709 88.266 1.00 74.08 C ANISOU 1536 CB MET A 250 10030 8291 9825 -756 343 612 C ATOM 1537 CG MET A 250 234.183 15.657 88.616 1.00 72.33 C ANISOU 1537 CG MET A 250 9672 8186 9624 -694 347 492 C ATOM 1538 SD MET A 250 235.518 15.480 87.418 1.00 70.66 S ANISOU 1538 SD MET A 250 9268 8281 9299 -822 353 364 S ATOM 1539 CE MET A 250 236.431 14.123 88.149 1.00 74.40 C ANISOU 1539 CE MET A 250 9608 8815 9846 -645 312 194 C ATOM 1540 N LEU A 251 233.867 19.205 90.054 1.00 78.93 N ANISOU 1540 N LEU A 251 10911 8733 10347 -888 250 739 N ATOM 1541 CA LEU A 251 234.796 19.943 90.901 1.00 79.41 C ANISOU 1541 CA LEU A 251 11027 8793 10353 -960 218 753 C ATOM 1542 C LEU A 251 234.125 20.394 92.194 1.00 79.82 C ANISOU 1542 C LEU A 251 11201 8659 10470 -841 193 785 C ATOM 1543 O LEU A 251 234.704 20.262 93.276 1.00 85.80 O ANISOU 1543 O LEU A 251 11948 9413 11240 -804 204 762 O ATOM 1544 CB LEU A 251 235.371 21.136 90.139 1.00 73.83 C ANISOU 1544 CB LEU A 251 10404 8139 9509 -1189 152 816 C ATOM 1545 CG LEU A 251 236.356 20.766 89.028 1.00 73.15 C ANISOU 1545 CG LEU A 251 10163 8321 9311 -1359 186 760 C ATOM 1546 CD1 LEU A 251 236.823 22.002 88.274 1.00 78.05 C ANISOU 1546 CD1 LEU A 251 10895 8999 9763 -1644 106 847 C ATOM 1547 CD2 LEU A 251 237.541 19.992 89.591 1.00 69.64 C ANISOU 1547 CD2 LEU A 251 9545 8055 8861 -1322 236 638 C ATOM 1548 N VAL A 252 232.899 20.915 92.109 1.00 74.65 N ANISOU 1548 N VAL A 252 10648 7865 9849 -774 154 821 N ATOM 1549 CA VAL A 252 232.216 21.367 93.317 1.00 69.43 C ANISOU 1549 CA VAL A 252 10074 7073 9235 -654 128 814 C ATOM 1550 C VAL A 252 231.854 20.183 94.207 1.00 66.46 C ANISOU 1550 C VAL A 252 9600 6725 8925 -531 210 767 C ATOM 1551 O VAL A 252 231.999 20.248 95.433 1.00 64.02 O ANISOU 1551 O VAL A 252 9313 6387 8624 -488 215 753 O ATOM 1552 CB VAL A 252 230.979 22.208 92.955 1.00 65.67 C ANISOU 1552 CB VAL A 252 9708 6470 8772 -590 46 824 C ATOM 1553 CG1 VAL A 252 230.196 22.570 94.210 1.00 60.44 C ANISOU 1553 CG1 VAL A 252 9088 5726 8151 -443 25 769 C ATOM 1554 CG2 VAL A 252 231.398 23.473 92.219 1.00 71.63 C ANISOU 1554 CG2 VAL A 252 10616 7151 9448 -735 -86 890 C ATOM 1555 N ILE A 253 231.388 19.082 93.611 1.00 67.48 N ANISOU 1555 N ILE A 253 9636 6911 9094 -491 263 748 N ATOM 1556 CA ILE A 253 231.003 17.916 94.405 1.00 65.97 C ANISOU 1556 CA ILE A 253 9387 6731 8949 -411 310 721 C ATOM 1557 C ILE A 253 232.214 17.333 95.121 1.00 65.58 C ANISOU 1557 C ILE A 253 9302 6717 8898 -429 306 703 C ATOM 1558 O ILE A 253 232.201 17.141 96.341 1.00 64.26 O ANISOU 1558 O ILE A 253 9165 6515 8737 -398 304 704 O ATOM 1559 CB ILE A 253 230.321 16.854 93.524 1.00 66.12 C ANISOU 1559 CB ILE A 253 9332 6788 9003 -382 343 710 C ATOM 1560 CG1 ILE A 253 228.989 17.356 92.974 1.00 64.79 C ANISOU 1560 CG1 ILE A 253 9191 6590 8838 -345 345 716 C ATOM 1561 CG2 ILE A 253 230.105 15.569 94.301 1.00 65.48 C ANISOU 1561 CG2 ILE A 253 9222 6706 8952 -342 357 697 C ATOM 1562 CD1 ILE A 253 228.554 16.590 91.756 1.00 63.42 C ANISOU 1562 CD1 ILE A 253 8950 6462 8686 -348 370 713 C ATOM 1563 N SER A 254 233.279 17.043 94.371 1.00 66.12 N ANISOU 1563 N SER A 254 9298 6875 8951 -480 297 672 N ATOM 1564 CA SER A 254 234.409 16.325 94.950 1.00 64.71 C ANISOU 1564 CA SER A 254 9063 6746 8779 -463 274 620 C ATOM 1565 C SER A 254 235.204 17.189 95.923 1.00 65.50 C ANISOU 1565 C SER A 254 9216 6834 8837 -507 256 634 C ATOM 1566 O SER A 254 235.749 16.668 96.902 1.00 65.37 O ANISOU 1566 O SER A 254 9196 6803 8838 -466 230 611 O ATOM 1567 CB SER A 254 235.312 15.790 93.839 1.00 66.48 C ANISOU 1567 CB SER A 254 9159 7117 8986 -489 264 538 C ATOM 1568 OG SER A 254 235.604 16.798 92.889 1.00 67.32 O ANISOU 1568 OG SER A 254 9255 7313 9012 -617 281 556 O ATOM 1569 N ILE A 255 235.279 18.500 95.687 1.00 65.44 N ANISOU 1569 N ILE A 255 9275 6818 8772 -595 250 676 N ATOM 1570 CA ILE A 255 236.032 19.365 96.591 1.00 63.73 C ANISOU 1570 CA ILE A 255 9122 6583 8510 -647 224 692 C ATOM 1571 C ILE A 255 235.290 19.533 97.913 1.00 66.67 C ANISOU 1571 C ILE A 255 9579 6836 8918 -565 223 715 C ATOM 1572 O ILE A 255 235.858 19.322 98.991 1.00 68.74 O ANISOU 1572 O ILE A 255 9844 7094 9181 -548 216 703 O ATOM 1573 CB ILE A 255 236.321 20.725 95.930 1.00 60.70 C ANISOU 1573 CB ILE A 255 8818 6204 8041 -790 184 739 C ATOM 1574 CG1 ILE A 255 237.402 20.576 94.856 1.00 62.36 C ANISOU 1574 CG1 ILE A 255 8919 6605 8171 -927 190 703 C ATOM 1575 CG2 ILE A 255 236.735 21.748 96.973 1.00 59.66 C ANISOU 1575 CG2 ILE A 255 8797 5998 7874 -827 140 768 C ATOM 1576 CD1 ILE A 255 237.643 21.835 94.054 1.00 62.42 C ANISOU 1576 CD1 ILE A 255 9022 6631 8064 -1125 136 769 C ATOM 1577 N LEU A 256 234.011 19.912 97.852 1.00 65.59 N ANISOU 1577 N LEU A 256 9499 6622 8800 -513 226 733 N ATOM 1578 CA LEU A 256 233.259 20.156 99.079 1.00 62.74 C ANISOU 1578 CA LEU A 256 9189 6202 8448 -444 229 723 C ATOM 1579 C LEU A 256 233.089 18.879 99.894 1.00 66.53 C ANISOU 1579 C LEU A 256 9617 6712 8950 -409 264 714 C ATOM 1580 O LEU A 256 233.154 18.914 101.128 1.00 69.62 O ANISOU 1580 O LEU A 256 10037 7095 9322 -405 262 710 O ATOM 1581 CB LEU A 256 231.898 20.772 98.756 1.00 58.41 C ANISOU 1581 CB LEU A 256 8681 5606 7908 -379 214 703 C ATOM 1582 CG LEU A 256 231.917 22.186 98.172 1.00 58.78 C ANISOU 1582 CG LEU A 256 8837 5569 7929 -404 124 714 C ATOM 1583 CD1 LEU A 256 230.505 22.668 97.881 1.00 59.70 C ANISOU 1583 CD1 LEU A 256 8984 5635 8066 -299 82 665 C ATOM 1584 CD2 LEU A 256 232.636 23.147 99.107 1.00 59.20 C ANISOU 1584 CD2 LEU A 256 8980 5565 7946 -434 67 715 C ATOM 1585 N ASN A 257 232.874 17.742 99.229 1.00 68.01 N ANISOU 1585 N ASN A 257 9742 6928 9169 -397 279 713 N ATOM 1586 CA ASN A 257 232.720 16.492 99.967 1.00 71.38 C ANISOU 1586 CA ASN A 257 10159 7354 9607 -388 271 720 C ATOM 1587 C ASN A 257 234.020 16.097 100.656 1.00 73.90 C ANISOU 1587 C ASN A 257 10484 7665 9928 -399 218 712 C ATOM 1588 O ASN A 257 233.999 15.540 101.760 1.00 77.52 O ANISOU 1588 O ASN A 257 10986 8095 10373 -412 188 732 O ATOM 1589 CB ASN A 257 232.242 15.376 99.037 1.00 74.49 C ANISOU 1589 CB ASN A 257 10507 7758 10037 -372 269 717 C ATOM 1590 CG ASN A 257 230.803 15.564 98.591 1.00 76.99 C ANISOU 1590 CG ASN A 257 10816 8094 10345 -362 318 722 C ATOM 1591 OD1 ASN A 257 230.079 16.407 99.122 1.00 78.20 O ANISOU 1591 OD1 ASN A 257 10990 8260 10463 -352 344 710 O ATOM 1592 ND2 ASN A 257 230.380 14.770 97.615 1.00 79.74 N ANISOU 1592 ND2 ASN A 257 11123 8452 10722 -352 322 721 N ATOM 1593 N THR A 258 235.161 16.381 100.025 1.00 72.52 N ANISOU 1593 N THR A 258 10263 7535 9758 -407 200 678 N ATOM 1594 CA THR A 258 236.441 16.104 100.670 1.00 70.91 C ANISOU 1594 CA THR A 258 10043 7348 9549 -404 145 645 C ATOM 1595 C THR A 258 236.637 16.991 101.893 1.00 71.04 C ANISOU 1595 C THR A 258 10131 7334 9526 -438 153 676 C ATOM 1596 O THR A 258 237.206 16.554 102.901 1.00 72.76 O ANISOU 1596 O THR A 258 10374 7531 9742 -430 105 674 O ATOM 1597 CB THR A 258 237.586 16.298 99.677 1.00 69.58 C ANISOU 1597 CB THR A 258 9776 7295 9365 -425 135 576 C ATOM 1598 OG1 THR A 258 237.345 15.504 98.510 1.00 71.70 O ANISOU 1598 OG1 THR A 258 9967 7609 9666 -389 131 531 O ATOM 1599 CG2 THR A 258 238.904 15.866 100.297 1.00 67.42 C ANISOU 1599 CG2 THR A 258 9458 7071 9089 -396 66 507 C ATOM 1600 N VAL A 259 236.162 18.236 101.826 1.00 69.37 N ANISOU 1600 N VAL A 259 9965 7110 9284 -470 193 700 N ATOM 1601 CA VAL A 259 236.241 19.128 102.977 1.00 68.25 C ANISOU 1601 CA VAL A 259 9894 6934 9105 -488 192 714 C ATOM 1602 C VAL A 259 235.308 18.654 104.087 1.00 70.87 C ANISOU 1602 C VAL A 259 10256 7244 9428 -466 205 725 C ATOM 1603 O VAL A 259 235.638 18.746 105.276 1.00 74.74 O ANISOU 1603 O VAL A 259 10782 7727 9888 -486 191 731 O ATOM 1604 CB VAL A 259 235.931 20.574 102.547 1.00 64.06 C ANISOU 1604 CB VAL A 259 9423 6370 8546 -512 189 720 C ATOM 1605 CG1 VAL A 259 235.908 21.500 103.751 1.00 70.68 C ANISOU 1605 CG1 VAL A 259 10339 7164 9352 -509 171 713 C ATOM 1606 CG2 VAL A 259 236.950 21.052 101.530 1.00 60.13 C ANISOU 1606 CG2 VAL A 259 8909 5919 8018 -598 166 725 C ATOM 1607 N ILE A 260 234.135 18.131 103.718 1.00 69.52 N ANISOU 1607 N ILE A 260 10066 7083 9267 -446 233 728 N ATOM 1608 CA ILE A 260 233.194 17.627 104.715 1.00 66.67 C ANISOU 1608 CA ILE A 260 9719 6751 8862 -470 250 735 C ATOM 1609 C ILE A 260 233.777 16.422 105.442 1.00 64.00 C ANISOU 1609 C ILE A 260 9411 6389 8516 -519 191 776 C ATOM 1610 O ILE A 260 233.597 16.264 106.656 1.00 61.55 O ANISOU 1610 O ILE A 260 9142 6100 8144 -581 181 796 O ATOM 1611 CB ILE A 260 231.845 17.292 104.052 1.00 66.95 C ANISOU 1611 CB ILE A 260 9714 6829 8894 -457 290 722 C ATOM 1612 CG1 ILE A 260 231.164 18.561 103.536 1.00 67.71 C ANISOU 1612 CG1 ILE A 260 9798 6936 8992 -391 314 665 C ATOM 1613 CG2 ILE A 260 230.928 16.568 105.025 1.00 68.05 C ANISOU 1613 CG2 ILE A 260 9854 7045 8958 -532 306 731 C ATOM 1614 CD1 ILE A 260 229.899 18.290 102.751 1.00 67.92 C ANISOU 1614 CD1 ILE A 260 9773 7012 9022 -361 347 638 C ATOM 1615 N ALA A 261 234.494 15.558 104.717 1.00 69.89 N ANISOU 1615 N ALA A 261 10143 7094 9319 -492 132 779 N ATOM 1616 CA ALA A 261 235.063 14.364 105.334 1.00 75.26 C ANISOU 1616 CA ALA A 261 10876 7716 10003 -512 25 804 C ATOM 1617 C ALA A 261 236.104 14.723 106.388 1.00 79.92 C ANISOU 1617 C ALA A 261 11501 8291 10573 -522 -18 802 C ATOM 1618 O ALA A 261 236.217 14.045 107.416 1.00 83.80 O ANISOU 1618 O ALA A 261 12072 8738 11030 -576 -98 843 O ATOM 1619 CB ALA A 261 235.674 13.460 104.263 1.00 75.72 C ANISOU 1619 CB ALA A 261 10896 7741 10135 -440 -52 763 C ATOM 1620 N ASN A 262 236.875 15.786 106.152 1.00 81.18 N ANISOU 1620 N ASN A 262 11614 8488 10742 -491 24 762 N ATOM 1621 CA ASN A 262 237.883 16.186 107.128 1.00 83.49 C ANISOU 1621 CA ASN A 262 11933 8779 11012 -505 -11 756 C ATOM 1622 C ASN A 262 237.240 16.756 108.386 1.00 85.53 C ANISOU 1622 C ASN A 262 12252 9045 11200 -570 31 793 C ATOM 1623 O ASN A 262 237.658 16.431 109.503 1.00 87.71 O ANISOU 1623 O ASN A 262 12584 9301 11443 -611 -26 819 O ATOM 1624 CB ASN A 262 238.849 17.196 106.507 1.00 82.72 C ANISOU 1624 CB ASN A 262 11774 8737 10919 -490 20 708 C ATOM 1625 CG ASN A 262 239.792 16.560 105.501 1.00 82.10 C ANISOU 1625 CG ASN A 262 11605 8710 10881 -440 -33 638 C ATOM 1626 OD1 ASN A 262 240.060 15.359 105.558 1.00 83.25 O ANISOU 1626 OD1 ASN A 262 11746 8821 11064 -382 -130 608 O ATOM 1627 ND2 ASN A 262 240.300 17.364 104.575 1.00 82.53 N ANISOU 1627 ND2 ASN A 262 11589 8853 10914 -469 12 601 N ATOM 1628 N LYS A 263 236.214 17.598 108.226 1.00 82.05 N ANISOU 1628 N LYS A 263 11797 8645 10733 -574 116 781 N ATOM 1629 CA LYS A 263 235.568 18.204 109.387 1.00 76.27 C ANISOU 1629 CA LYS A 263 11091 7961 9927 -618 155 773 C ATOM 1630 C LYS A 263 234.912 17.151 110.270 1.00 76.90 C ANISOU 1630 C LYS A 263 11204 8078 9937 -714 132 817 C ATOM 1631 O LYS A 263 234.976 17.235 111.502 1.00 79.81 O ANISOU 1631 O LYS A 263 11608 8485 10231 -787 122 829 O ATOM 1632 CB LYS A 263 234.538 19.240 108.939 1.00 68.44 C ANISOU 1632 CB LYS A 263 10065 7012 8926 -569 220 714 C ATOM 1633 CG LYS A 263 233.950 20.057 110.079 1.00 65.26 C ANISOU 1633 CG LYS A 263 9664 6683 8448 -578 247 654 C ATOM 1634 CD LYS A 263 234.962 21.056 110.613 1.00 64.51 C ANISOU 1634 CD LYS A 263 9617 6536 8356 -563 218 641 C ATOM 1635 CE LYS A 263 234.450 21.765 111.860 1.00 66.87 C ANISOU 1635 CE LYS A 263 9913 6917 8577 -567 235 567 C ATOM 1636 NZ LYS A 263 233.384 22.758 111.554 1.00 69.12 N ANISOU 1636 NZ LYS A 263 10167 7237 8857 -468 241 451 N ATOM 1637 N LEU A 264 234.275 16.151 109.659 1.00 74.21 N ANISOU 1637 N LEU A 264 10861 7731 9605 -739 114 847 N ATOM 1638 CA LEU A 264 233.663 15.087 110.446 1.00 74.66 C ANISOU 1638 CA LEU A 264 10977 7818 9574 -876 68 909 C ATOM 1639 C LEU A 264 234.718 14.259 111.167 1.00 72.40 C ANISOU 1639 C LEU A 264 10795 7425 9289 -922 -69 972 C ATOM 1640 O LEU A 264 234.487 13.790 112.287 1.00 79.96 O ANISOU 1640 O LEU A 264 11829 8409 10142 -1066 -120 1030 O ATOM 1641 CB LEU A 264 232.797 14.200 109.551 1.00 71.94 C ANISOU 1641 CB LEU A 264 10623 7473 9237 -900 61 932 C ATOM 1642 CG LEU A 264 231.490 14.811 109.036 1.00 65.45 C ANISOU 1642 CG LEU A 264 9703 6783 8383 -884 181 869 C ATOM 1643 CD1 LEU A 264 230.850 13.896 108.009 1.00 62.62 C ANISOU 1643 CD1 LEU A 264 9338 6404 8051 -895 166 897 C ATOM 1644 CD2 LEU A 264 230.530 15.080 110.187 1.00 65.38 C ANISOU 1644 CD2 LEU A 264 9662 6956 8224 -1008 238 838 C ATOM 1645 N THR A 265 235.883 14.069 110.545 1.00 63.67 N ANISOU 1645 N THR A 265 9688 6214 8288 -807 -143 952 N ATOM 1646 CA THR A 265 236.954 13.345 111.219 1.00 61.51 C ANISOU 1646 CA THR A 265 9504 5840 8026 -812 -298 980 C ATOM 1647 C THR A 265 237.544 14.175 112.352 1.00 62.97 C ANISOU 1647 C THR A 265 9700 6063 8162 -843 -272 977 C ATOM 1648 O THR A 265 237.932 13.633 113.393 1.00 68.18 O ANISOU 1648 O THR A 265 10460 6674 8773 -921 -383 1029 O ATOM 1649 CB THR A 265 238.036 12.948 110.215 1.00 65.24 C ANISOU 1649 CB THR A 265 9933 6241 8615 -661 -384 912 C ATOM 1650 OG1 THR A 265 237.436 12.224 109.136 1.00 67.94 O ANISOU 1650 OG1 THR A 265 10259 6555 9001 -629 -402 905 O ATOM 1651 CG2 THR A 265 239.081 12.061 110.879 1.00 65.80 C ANISOU 1651 CG2 THR A 265 10096 6200 8704 -635 -585 913 C ATOM 1652 N VAL A 266 237.608 15.495 112.173 1.00 60.28 N ANISOU 1652 N VAL A 266 9274 5800 7831 -791 -144 920 N ATOM 1653 CA VAL A 266 238.070 16.366 113.250 1.00 60.58 C ANISOU 1653 CA VAL A 266 9323 5876 7817 -822 -116 911 C ATOM 1654 C VAL A 266 237.106 16.300 114.428 1.00 63.72 C ANISOU 1654 C VAL A 266 9763 6358 8091 -964 -88 947 C ATOM 1655 O VAL A 266 237.521 16.168 115.586 1.00 68.05 O ANISOU 1655 O VAL A 266 10376 6907 8574 -1047 -142 983 O ATOM 1656 CB VAL A 266 238.247 17.807 112.738 1.00 59.81 C ANISOU 1656 CB VAL A 266 9154 5822 7751 -746 -14 843 C ATOM 1657 CG1 VAL A 266 238.451 18.766 113.897 1.00 60.36 C ANISOU 1657 CG1 VAL A 266 9245 5934 7757 -784 17 826 C ATOM 1658 CG2 VAL A 266 239.421 17.880 111.779 1.00 59.43 C ANISOU 1658 CG2 VAL A 266 9062 5736 7782 -664 -50 810 C ATOM 1659 N MET A 267 235.802 16.369 114.147 1.00 64.93 N ANISOU 1659 N MET A 267 9869 6607 8194 -1004 -4 929 N ATOM 1660 CA MET A 267 234.808 16.336 115.216 1.00 67.30 C ANISOU 1660 CA MET A 267 10169 7056 8345 -1157 37 933 C ATOM 1661 C MET A 267 234.860 15.030 115.994 1.00 65.06 C ANISOU 1661 C MET A 267 10008 6738 7974 -1338 -88 1046 C ATOM 1662 O MET A 267 234.603 15.018 117.203 1.00 66.35 O ANISOU 1662 O MET A 267 10203 7009 7999 -1497 -90 1070 O ATOM 1663 CB MET A 267 233.409 16.557 114.643 1.00 72.88 C ANISOU 1663 CB MET A 267 10780 7900 9013 -1158 137 869 C ATOM 1664 CG MET A 267 233.185 17.964 114.127 1.00 77.41 C ANISOU 1664 CG MET A 267 11259 8510 9644 -997 227 747 C ATOM 1665 SD MET A 267 233.516 19.206 115.389 1.00 78.50 S ANISOU 1665 SD MET A 267 11381 8725 9719 -984 255 664 S ATOM 1666 CE MET A 267 232.238 18.816 116.581 1.00 79.84 C ANISOU 1666 CE MET A 267 11485 9166 9684 -1172 306 618 C ATOM 1667 N VAL A 268 235.188 13.923 115.327 1.00 67.96 N ANISOU 1667 N VAL A 268 10457 6956 8410 -1323 -210 1113 N ATOM 1668 CA VAL A 268 235.347 12.661 116.039 1.00 74.28 C ANISOU 1668 CA VAL A 268 11420 7666 9135 -1487 -387 1227 C ATOM 1669 C VAL A 268 236.616 12.686 116.882 1.00 79.61 C ANISOU 1669 C VAL A 268 12178 8238 9833 -1462 -501 1250 C ATOM 1670 O VAL A 268 236.638 12.190 118.015 1.00 85.39 O ANISOU 1670 O VAL A 268 13031 8967 10445 -1643 -604 1334 O ATOM 1671 CB VAL A 268 235.341 11.486 115.045 1.00 76.27 C ANISOU 1671 CB VAL A 268 11749 7764 9468 -1448 -520 1270 C ATOM 1672 CG1 VAL A 268 235.664 10.180 115.756 1.00 81.04 C ANISOU 1672 CG1 VAL A 268 12567 8214 10012 -1596 -765 1387 C ATOM 1673 CG2 VAL A 268 233.995 11.395 114.349 1.00 73.25 C ANISOU 1673 CG2 VAL A 268 11294 7499 9038 -1510 -409 1260 C ATOM 1674 N ASN A1002 237.687 13.280 116.352 1.00 77.79 N ANISOU 1674 N ASN A1002 11880 7940 9737 -1259 -488 1174 N ATOM 1675 CA ASN A1002 238.939 13.343 117.096 1.00 77.30 C ANISOU 1675 CA ASN A1002 11874 7800 9698 -1220 -592 1176 C ATOM 1676 C ASN A1002 238.844 14.327 118.255 1.00 79.56 C ANISOU 1676 C ASN A1002 12132 8216 9880 -1313 -486 1170 C ATOM 1677 O ASN A1002 239.202 13.998 119.391 1.00 86.53 O ANISOU 1677 O ASN A1002 13118 9076 10682 -1430 -587 1232 O ATOM 1678 CB ASN A1002 240.086 13.721 116.159 1.00 77.97 C ANISOU 1678 CB ASN A1002 11867 7829 9929 -1003 -597 1080 C ATOM 1679 CG ASN A1002 240.398 12.633 115.153 1.00 82.67 C ANISOU 1679 CG ASN A1002 12486 8304 10622 -896 -740 1057 C ATOM 1680 OD1 ASN A1002 240.628 12.908 113.977 1.00 84.31 O ANISOU 1680 OD1 ASN A1002 12577 8539 10919 -762 -677 975 O ATOM 1681 ND2 ASN A1002 240.406 11.389 115.612 1.00 86.21 N ANISOU 1681 ND2 ASN A1002 13094 8616 11045 -964 -951 1128 N ATOM 1682 N ILE A1003 238.355 15.542 117.989 1.00 74.87 N ANISOU 1682 N ILE A1003 11409 7751 9287 -1258 -303 1089 N ATOM 1683 CA ILE A1003 238.306 16.567 119.027 1.00 72.26 C ANISOU 1683 CA ILE A1003 11043 7540 8871 -1310 -214 1050 C ATOM 1684 C ILE A1003 237.357 16.189 120.156 1.00 75.55 C ANISOU 1684 C ILE A1003 11500 8099 9108 -1533 -208 1096 C ATOM 1685 O ILE A1003 237.520 16.671 121.284 1.00 76.82 O ANISOU 1685 O ILE A1003 11665 8347 9175 -1616 -188 1086 O ATOM 1686 CB ILE A1003 237.915 17.931 118.424 1.00 66.91 C ANISOU 1686 CB ILE A1003 10242 6944 8238 -1186 -62 938 C ATOM 1687 CG1 ILE A1003 238.170 19.057 119.429 1.00 70.61 C ANISOU 1687 CG1 ILE A1003 10688 7491 8648 -1193 -8 879 C ATOM 1688 CG2 ILE A1003 236.452 17.944 118.007 1.00 66.35 C ANISOU 1688 CG2 ILE A1003 10100 6997 8112 -1219 28 897 C ATOM 1689 CD1 ILE A1003 239.572 19.071 119.983 1.00 71.18 C ANISOU 1689 CD1 ILE A1003 10823 7468 8753 -1181 -91 917 C ATOM 1690 N PHE A1004 236.374 15.327 119.888 1.00 77.92 N ANISOU 1690 N PHE A1004 11824 8444 9339 -1655 -225 1145 N ATOM 1691 CA PHE A1004 235.406 14.964 120.917 1.00 81.32 C ANISOU 1691 CA PHE A1004 12275 9062 9560 -1916 -212 1184 C ATOM 1692 C PHE A1004 236.079 14.211 122.056 1.00 81.18 C ANISOU 1692 C PHE A1004 12427 8967 9451 -2094 -378 1308 C ATOM 1693 O PHE A1004 236.024 14.633 123.217 1.00 83.98 O ANISOU 1693 O PHE A1004 12771 9467 9670 -2229 -342 1298 O ATOM 1694 CB PHE A1004 234.281 14.126 120.307 1.00 81.19 C ANISOU 1694 CB PHE A1004 12262 9107 9481 -2032 -213 1222 C ATOM 1695 CG PHE A1004 233.161 13.826 121.262 1.00 85.75 C ANISOU 1695 CG PHE A1004 12825 9948 9809 -2333 -176 1242 C ATOM 1696 CD1 PHE A1004 232.824 14.726 122.260 1.00 87.07 C ANISOU 1696 CD1 PHE A1004 12877 10363 9843 -2402 -60 1141 C ATOM 1697 CD2 PHE A1004 232.454 12.640 121.172 1.00 89.52 C ANISOU 1697 CD2 PHE A1004 13401 10442 10168 -2563 -267 1353 C ATOM 1698 CE1 PHE A1004 231.797 14.452 123.143 1.00 88.91 C ANISOU 1698 CE1 PHE A1004 13066 10898 9818 -2700 -19 1135 C ATOM 1699 CE2 PHE A1004 231.428 12.361 122.054 1.00 92.15 C ANISOU 1699 CE2 PHE A1004 13713 11063 10237 -2887 -231 1371 C ATOM 1700 CZ PHE A1004 231.099 13.268 123.040 1.00 91.16 C ANISOU 1700 CZ PHE A1004 13444 11223 9968 -2958 -99 1254 C ATOM 1701 N GLU A1005 236.734 13.092 121.741 1.00 81.70 N ANISOU 1701 N GLU A1005 12655 8798 9589 -2089 -579 1414 N ATOM 1702 CA GLU A1005 237.334 12.284 122.795 1.00 84.28 C ANISOU 1702 CA GLU A1005 13178 9017 9829 -2260 -785 1538 C ATOM 1703 C GLU A1005 238.541 12.970 123.418 1.00 84.25 C ANISOU 1703 C GLU A1005 13165 8958 9889 -2138 -800 1498 C ATOM 1704 O GLU A1005 238.781 12.819 124.620 1.00 90.38 O ANISOU 1704 O GLU A1005 14042 9761 10539 -2314 -882 1568 O ATOM 1705 CB GLU A1005 237.725 10.912 122.251 1.00 92.29 C ANISOU 1705 CB GLU A1005 14382 9767 10918 -2248 -1040 1635 C ATOM 1706 CG GLU A1005 236.537 10.019 121.964 1.00 99.57 C ANISOU 1706 CG GLU A1005 15379 10732 11723 -2462 -1081 1720 C ATOM 1707 CD GLU A1005 236.790 8.579 122.351 1.00104.86 C ANISOU 1707 CD GLU A1005 16339 11172 12331 -2639 -1407 1879 C ATOM 1708 OE1 GLU A1005 237.847 8.304 122.960 1.00109.75 O ANISOU 1708 OE1 GLU A1005 17096 11614 12989 -2597 -1602 1917 O ATOM 1709 OE2 GLU A1005 235.932 7.723 122.048 1.00106.18 O ANISOU 1709 OE2 GLU A1005 16607 11328 12409 -2822 -1486 1964 O ATOM 1710 N MET A1006 239.307 13.724 122.626 1.00 78.38 N ANISOU 1710 N MET A1006 12306 8151 9323 -1865 -725 1392 N ATOM 1711 CA MET A1006 240.482 14.397 123.167 1.00 77.39 C ANISOU 1711 CA MET A1006 12165 7988 9251 -1760 -737 1351 C ATOM 1712 C MET A1006 240.101 15.371 124.273 1.00 80.34 C ANISOU 1712 C MET A1006 12474 8562 9488 -1882 -596 1319 C ATOM 1713 O MET A1006 240.772 15.441 125.309 1.00 81.09 O ANISOU 1713 O MET A1006 12638 8645 9528 -1951 -666 1354 O ATOM 1714 CB MET A1006 241.231 15.125 122.053 1.00 78.54 C ANISOU 1714 CB MET A1006 12182 8084 9575 -1495 -660 1239 C ATOM 1715 CG MET A1006 241.898 14.210 121.052 1.00 78.29 C ANISOU 1715 CG MET A1006 12189 7880 9679 -1348 -814 1232 C ATOM 1716 SD MET A1006 242.880 15.131 119.860 1.00 77.36 S ANISOU 1716 SD MET A1006 11901 7773 9718 -1097 -717 1094 S ATOM 1717 CE MET A1006 243.351 13.814 118.740 1.00 77.64 C ANISOU 1717 CE MET A1006 11965 7660 9873 -956 -908 1065 C ATOM 1718 N LEU A1007 239.024 16.131 124.073 1.00 81.66 N ANISOU 1718 N LEU A1007 12505 8921 9601 -1897 -408 1236 N ATOM 1719 CA LEU A1007 238.616 17.105 125.077 1.00 81.05 C ANISOU 1719 CA LEU A1007 12343 9056 9396 -1979 -282 1162 C ATOM 1720 C LEU A1007 237.781 16.474 126.181 1.00 80.88 C ANISOU 1720 C LEU A1007 12374 9214 9142 -2288 -309 1230 C ATOM 1721 O LEU A1007 237.868 16.906 127.336 1.00 81.60 O ANISOU 1721 O LEU A1007 12456 9441 9108 -2406 -283 1211 O ATOM 1722 CB LEU A1007 237.845 18.250 124.419 1.00 78.71 C ANISOU 1722 CB LEU A1007 11875 8891 9140 -1836 -102 1007 C ATOM 1723 CG LEU A1007 238.715 19.187 123.584 1.00 73.77 C ANISOU 1723 CG LEU A1007 11207 8126 8697 -1585 -71 938 C ATOM 1724 CD1 LEU A1007 237.874 20.270 122.942 1.00 74.46 C ANISOU 1724 CD1 LEU A1007 11166 8311 8814 -1457 59 797 C ATOM 1725 CD2 LEU A1007 239.811 19.792 124.445 1.00 72.53 C ANISOU 1725 CD2 LEU A1007 11085 7931 8543 -1567 -101 933 C ATOM 1726 N ARG A1008 236.977 15.459 125.858 1.00 81.69 N ANISOU 1726 N ARG A1008 12534 9335 9168 -2443 -364 1310 N ATOM 1727 CA ARG A1008 236.203 14.789 126.893 1.00 86.76 C ANISOU 1727 CA ARG A1008 13242 10166 9555 -2795 -406 1393 C ATOM 1728 C ARG A1008 237.095 14.040 127.877 1.00 89.04 C ANISOU 1728 C ARG A1008 13748 10305 9778 -2961 -617 1548 C ATOM 1729 O ARG A1008 236.657 13.747 128.995 1.00 94.92 O ANISOU 1729 O ARG A1008 14548 11229 10288 -3274 -648 1613 O ATOM 1730 CB ARG A1008 235.184 13.836 126.263 1.00 90.32 C ANISOU 1730 CB ARG A1008 13728 10657 9933 -2945 -438 1457 C ATOM 1731 CG ARG A1008 235.584 12.371 126.277 1.00 94.33 C ANISOU 1731 CG ARG A1008 14501 10915 10425 -3104 -703 1658 C ATOM 1732 CD ARG A1008 234.382 11.480 126.012 1.00100.05 C ANISOU 1732 CD ARG A1008 15269 11756 10990 -3363 -728 1731 C ATOM 1733 NE ARG A1008 234.702 10.065 126.165 1.00104.57 N ANISOU 1733 NE ARG A1008 16138 12079 11517 -3558 -1023 1933 N ATOM 1734 CZ ARG A1008 233.802 9.089 126.111 1.00110.80 C ANISOU 1734 CZ ARG A1008 17043 12920 12135 -3856 -1117 2047 C ATOM 1735 NH1 ARG A1008 234.179 7.826 126.263 1.00116.18 N ANISOU 1735 NH1 ARG A1008 18033 13325 12786 -4020 -1432 2233 N ATOM 1736 NH2 ARG A1008 232.522 9.375 125.909 1.00111.40 N ANISOU 1736 NH2 ARG A1008 16934 13327 12066 -3991 -915 1967 N ATOM 1737 N ILE A1009 238.331 13.737 127.493 1.00 85.72 N ANISOU 1737 N ILE A1009 13442 9581 9548 -2765 -770 1597 N ATOM 1738 CA ILE A1009 239.291 13.121 128.404 1.00 84.33 C ANISOU 1738 CA ILE A1009 13466 9240 9334 -2868 -993 1717 C ATOM 1739 C ILE A1009 240.076 14.174 129.172 1.00 86.49 C ANISOU 1739 C ILE A1009 13658 9577 9626 -2776 -908 1640 C ATOM 1740 O ILE A1009 240.169 14.121 130.400 1.00 88.28 O ANISOU 1740 O ILE A1009 13962 9891 9688 -2992 -961 1702 O ATOM 1741 CB ILE A1009 240.235 12.180 127.625 1.00 83.15 C ANISOU 1741 CB ILE A1009 13472 8747 9373 -2687 -1234 1777 C ATOM 1742 CG1 ILE A1009 239.481 10.944 127.130 1.00 80.83 C ANISOU 1742 CG1 ILE A1009 13325 8362 9025 -2841 -1384 1886 C ATOM 1743 CG2 ILE A1009 241.425 11.788 128.488 1.00 85.34 C ANISOU 1743 CG2 ILE A1009 13922 8845 9659 -2696 -1464 1848 C ATOM 1744 CD1 ILE A1009 240.310 10.046 126.242 1.00 79.92 C ANISOU 1744 CD1 ILE A1009 13338 7922 9105 -2624 -1624 1901 C ATOM 1745 N ASP A1010 240.647 15.148 128.459 1.00 85.54 N ANISOU 1745 N ASP A1010 13392 9418 9692 -2475 -782 1508 N ATOM 1746 CA ASP A1010 241.490 16.150 129.105 1.00 84.04 C ANISOU 1746 CA ASP A1010 13141 9260 9531 -2380 -721 1438 C ATOM 1747 C ASP A1010 240.663 17.153 129.899 1.00 81.03 C ANISOU 1747 C ASP A1010 12622 9171 8994 -2495 -527 1343 C ATOM 1748 O ASP A1010 240.970 17.438 131.063 1.00 79.30 O ANISOU 1748 O ASP A1010 12430 9041 8662 -2618 -538 1353 O ATOM 1749 CB ASP A1010 242.342 16.875 128.065 1.00 87.84 C ANISOU 1749 CB ASP A1010 13521 9621 10231 -2066 -662 1335 C ATOM 1750 CG ASP A1010 243.278 15.949 127.333 1.00 89.83 C ANISOU 1750 CG ASP A1010 13869 9631 10629 -1930 -855 1382 C ATOM 1751 OD1 ASP A1010 243.684 14.927 127.928 1.00 94.47 O ANISOU 1751 OD1 ASP A1010 14629 10094 11172 -2035 -1074 1487 O ATOM 1752 OD2 ASP A1010 243.617 16.252 126.170 1.00 88.72 O ANISOU 1752 OD2 ASP A1010 13635 9433 10643 -1718 -803 1302 O ATOM 1753 N GLU A1011 239.621 17.717 129.279 1.00 80.38 N ANISOU 1753 N GLU A1011 12386 9249 8907 -2439 -358 1229 N ATOM 1754 CA GLU A1011 238.841 18.754 129.944 1.00 79.79 C ANISOU 1754 CA GLU A1011 12153 9462 8702 -2488 -189 1082 C ATOM 1755 C GLU A1011 237.840 18.165 130.928 1.00 81.66 C ANISOU 1755 C GLU A1011 12391 9968 8666 -2828 -185 1119 C ATOM 1756 O GLU A1011 237.485 18.820 131.916 1.00 83.71 O ANISOU 1756 O GLU A1011 12552 10485 8771 -2933 -95 1017 O ATOM 1757 CB GLU A1011 238.117 19.618 128.909 1.00 76.87 C ANISOU 1757 CB GLU A1011 11619 9159 8430 -2277 -42 921 C ATOM 1758 CG GLU A1011 237.563 20.922 129.464 1.00 81.98 C ANISOU 1758 CG GLU A1011 12103 10042 9003 -2219 96 720 C ATOM 1759 CD GLU A1011 238.634 21.981 129.680 1.00 88.74 C ANISOU 1759 CD GLU A1011 12972 10769 9974 -2041 94 665 C ATOM 1760 OE1 GLU A1011 239.754 21.817 129.158 1.00 93.41 O ANISOU 1760 OE1 GLU A1011 13664 11108 10720 -1933 14 761 O ATOM 1761 OE2 GLU A1011 238.358 22.993 130.357 1.00 90.12 O ANISOU 1761 OE2 GLU A1011 13050 11112 10081 -2009 166 510 O ATOM 1762 N GLY A1012 237.383 16.939 130.684 1.00 81.43 N ANISOU 1762 N GLY A1012 12476 9902 8563 -3018 -289 1257 N ATOM 1763 CA GLY A1012 236.478 16.266 131.594 1.00 84.93 C ANISOU 1763 CA GLY A1012 12948 10605 8716 -3403 -310 1322 C ATOM 1764 C GLY A1012 235.008 16.523 131.332 1.00 89.89 C ANISOU 1764 C GLY A1012 13374 11575 9205 -3486 -141 1179 C ATOM 1765 O GLY A1012 234.606 17.651 131.030 1.00 89.08 O ANISOU 1765 O GLY A1012 13060 11621 9165 -3267 26 966 O ATOM 1766 N LEU A1013 234.195 15.477 131.454 1.00 93.19 N ANISOU 1766 N LEU A1013 13863 12121 9425 -3809 -203 1291 N ATOM 1767 CA LEU A1013 232.749 15.563 131.296 1.00 95.82 C ANISOU 1767 CA LEU A1013 13999 12832 9577 -3949 -55 1159 C ATOM 1768 C LEU A1013 232.097 15.487 132.669 1.00 99.28 C ANISOU 1768 C LEU A1013 14370 13693 9657 -4352 -15 1132 C ATOM 1769 O LEU A1013 232.236 14.478 133.370 1.00105.25 O ANISOU 1769 O LEU A1013 15335 14428 10227 -4720 -175 1343 O ATOM 1770 CB LEU A1013 232.228 14.447 130.392 1.00 92.07 C ANISOU 1770 CB LEU A1013 13635 12242 9108 -4056 -143 1293 C ATOM 1771 CG LEU A1013 230.707 14.310 130.319 1.00 94.10 C ANISOU 1771 CG LEU A1013 13709 12917 9129 -4281 -14 1187 C ATOM 1772 CD1 LEU A1013 230.071 15.586 129.798 1.00 92.28 C ANISOU 1772 CD1 LEU A1013 13167 12906 8988 -3966 204 888 C ATOM 1773 CD2 LEU A1013 230.328 13.129 129.444 1.00 96.89 C ANISOU 1773 CD2 LEU A1013 14214 13105 9495 -4401 -130 1352 C ATOM 1774 N ARG A1014 231.388 16.549 133.048 1.00 97.83 N ANISOU 1774 N ARG A1014 13901 13899 9371 -4288 178 863 N ATOM 1775 CA ARG A1014 230.724 16.629 134.343 1.00 96.19 C ANISOU 1775 CA ARG A1014 13565 14173 8809 -4649 246 775 C ATOM 1776 C ARG A1014 229.320 17.174 134.133 1.00 94.64 C ANISOU 1776 C ARG A1014 13039 14458 8463 -4641 435 486 C ATOM 1777 O ARG A1014 229.153 18.276 133.599 1.00 90.66 O ANISOU 1777 O ARG A1014 12337 13973 8136 -4249 549 236 O ATOM 1778 CB ARG A1014 231.514 17.511 135.314 1.00 99.67 C ANISOU 1778 CB ARG A1014 13975 14630 9265 -4553 268 692 C ATOM 1779 CG ARG A1014 232.877 16.942 135.683 1.00100.48 C ANISOU 1779 CG ARG A1014 14388 14316 9474 -4598 72 962 C ATOM 1780 CD ARG A1014 233.669 17.890 136.567 1.00105.21 C ANISOU 1780 CD ARG A1014 14943 14926 10104 -4476 106 868 C ATOM 1781 NE ARG A1014 235.014 17.387 136.832 1.00104.58 N ANISOU 1781 NE ARG A1014 15144 14441 10149 -4474 -86 1105 N ATOM 1782 CZ ARG A1014 236.046 17.550 136.008 1.00103.93 C ANISOU 1782 CZ ARG A1014 15169 13931 10389 -4123 -156 1159 C ATOM 1783 NH1 ARG A1014 235.888 18.203 134.865 1.00 99.17 N ANISOU 1783 NH1 ARG A1014 14438 13235 10009 -3773 -51 1019 N ATOM 1784 NH2 ARG A1014 237.236 17.059 136.325 1.00106.17 N ANISOU 1784 NH2 ARG A1014 15684 13897 10758 -4131 -340 1345 N ATOM 1785 N LEU A1015 228.316 16.401 134.552 1.00 96.15 N ANISOU 1785 N LEU A1015 13176 15039 8317 -5080 450 514 N ATOM 1786 CA LEU A1015 226.921 16.765 134.340 1.00 97.87 C ANISOU 1786 CA LEU A1015 13066 15762 8359 -5109 620 233 C ATOM 1787 C LEU A1015 226.385 17.727 135.392 1.00 97.66 C ANISOU 1787 C LEU A1015 12726 16278 8103 -5153 765 -91 C ATOM 1788 O LEU A1015 225.256 18.209 135.247 1.00 98.28 O ANISOU 1788 O LEU A1015 12484 16808 8050 -5104 904 -398 O ATOM 1789 CB LEU A1015 226.053 15.505 134.305 1.00 95.67 C ANISOU 1789 CB LEU A1015 12851 15706 7792 -5591 574 394 C ATOM 1790 CG LEU A1015 226.398 14.488 133.216 1.00 94.76 C ANISOU 1790 CG LEU A1015 13028 15098 7880 -5558 420 681 C ATOM 1791 CD1 LEU A1015 225.494 13.268 133.307 1.00 98.64 C ANISOU 1791 CD1 LEU A1015 13596 15838 8047 -6083 358 838 C ATOM 1792 CD2 LEU A1015 226.313 15.125 131.837 1.00 89.39 C ANISOU 1792 CD2 LEU A1015 12230 14192 7541 -5042 501 531 C ATOM 1793 N LYS A1016 227.153 18.013 136.439 1.00 96.76 N ANISOU 1793 N LYS A1016 12685 16147 7934 -5233 728 -51 N ATOM 1794 CA LYS A1016 226.770 18.975 137.460 1.00 96.91 C ANISOU 1794 CA LYS A1016 12413 16652 7756 -5241 853 -370 C ATOM 1795 C LYS A1016 227.687 20.189 137.399 1.00 93.58 C ANISOU 1795 C LYS A1016 11989 15916 7650 -4749 855 -501 C ATOM 1796 O LYS A1016 228.761 20.158 136.791 1.00 88.10 O ANISOU 1796 O LYS A1016 11547 14653 7275 -4503 753 -294 O ATOM 1797 CB LYS A1016 226.825 18.351 138.860 1.00 95.87 C ANISOU 1797 CB LYS A1016 12349 16834 7244 -5795 813 -234 C ATOM 1798 CG LYS A1016 226.647 16.844 138.886 1.00 95.27 C ANISOU 1798 CG LYS A1016 12529 16716 6953 -6315 682 118 C ATOM 1799 CD LYS A1016 226.945 16.286 140.267 1.00 96.84 C ANISOU 1799 CD LYS A1016 12869 17110 6816 -6841 593 297 C ATOM 1800 CE LYS A1016 227.047 14.771 140.240 1.00 97.82 C ANISOU 1800 CE LYS A1016 13359 17016 6791 -7315 382 707 C ATOM 1801 NZ LYS A1016 227.377 14.218 141.583 1.00100.13 N ANISOU 1801 NZ LYS A1016 13805 17403 6838 -7776 224 870 N ATOM 1802 N ILE A1017 227.247 21.270 138.043 1.00 97.13 N ANISOU 1802 N ILE A1017 12145 16764 7995 -4616 964 -864 N ATOM 1803 CA ILE A1017 228.036 22.495 138.076 1.00 95.90 C ANISOU 1803 CA ILE A1017 11984 16347 8105 -4176 953 -1013 C ATOM 1804 C ILE A1017 229.247 22.295 138.976 1.00 99.66 C ANISOU 1804 C ILE A1017 12698 16588 8580 -4338 867 -770 C ATOM 1805 O ILE A1017 229.118 21.894 140.140 1.00102.80 O ANISOU 1805 O ILE A1017 13068 17332 8661 -4745 878 -735 O ATOM 1806 CB ILE A1017 227.177 23.676 138.551 1.00 90.84 C ANISOU 1806 CB ILE A1017 10967 16206 7342 -3984 1062 -1495 C ATOM 1807 CG1 ILE A1017 226.064 23.966 137.545 1.00 89.94 C ANISOU 1807 CG1 ILE A1017 10630 16260 7282 -3741 1117 -1754 C ATOM 1808 CG2 ILE A1017 228.038 24.909 138.767 1.00 94.24 C ANISOU 1808 CG2 ILE A1017 11429 16368 8008 -3590 1021 -1630 C ATOM 1809 CD1 ILE A1017 225.162 25.100 137.957 1.00 90.91 C ANISOU 1809 CD1 ILE A1017 10371 16881 7289 -3514 1190 -2270 C ATOM 1810 N TYR A1018 230.434 22.573 138.438 1.00 98.98 N ANISOU 1810 N TYR A1018 12842 15933 8834 -4035 776 -605 N ATOM 1811 CA TYR A1018 231.676 22.463 139.187 1.00100.30 C ANISOU 1811 CA TYR A1018 13232 15837 9041 -4124 683 -391 C ATOM 1812 C TYR A1018 232.489 23.739 139.020 1.00104.06 C ANISOU 1812 C TYR A1018 13706 16036 9795 -3683 679 -532 C ATOM 1813 O TYR A1018 232.248 24.542 138.114 1.00105.09 O ANISOU 1813 O TYR A1018 13746 16050 10135 -3308 707 -715 O ATOM 1814 CB TYR A1018 232.501 21.241 138.748 1.00 97.93 C ANISOU 1814 CB TYR A1018 13270 15090 8850 -4274 532 15 C ATOM 1815 CG TYR A1018 233.019 21.304 137.329 1.00 97.48 C ANISOU 1815 CG TYR A1018 13335 14547 9156 -3901 482 101 C ATOM 1816 CD1 TYR A1018 232.183 21.044 136.251 1.00 97.37 C ANISOU 1816 CD1 TYR A1018 13245 14554 9198 -3815 523 54 C ATOM 1817 CD2 TYR A1018 234.351 21.601 137.067 1.00 93.93 C ANISOU 1817 CD2 TYR A1018 13069 13644 8976 -3656 394 227 C ATOM 1818 CE1 TYR A1018 232.653 21.091 134.951 1.00 97.00 C ANISOU 1818 CE1 TYR A1018 13304 14087 9464 -3497 478 131 C ATOM 1819 CE2 TYR A1018 234.831 21.651 135.769 1.00 93.56 C ANISOU 1819 CE2 TYR A1018 13116 13203 9231 -3350 352 295 C ATOM 1820 CZ TYR A1018 233.976 21.395 134.715 1.00 93.80 C ANISOU 1820 CZ TYR A1018 13072 13259 9309 -3274 395 250 C ATOM 1821 OH TYR A1018 234.441 21.441 133.420 1.00 92.61 O ANISOU 1821 OH TYR A1018 13008 12739 9441 -2989 355 315 O ATOM 1822 N LYS A1019 233.460 23.915 139.913 1.00105.44 N ANISOU 1822 N LYS A1019 13999 16103 9959 -3751 628 -437 N ATOM 1823 CA LYS A1019 234.260 25.131 139.973 1.00107.98 C ANISOU 1823 CA LYS A1019 14326 16208 10493 -3402 617 -566 C ATOM 1824 C LYS A1019 235.511 24.988 139.114 1.00108.87 C ANISOU 1824 C LYS A1019 14701 15741 10922 -3195 511 -314 C ATOM 1825 O LYS A1019 236.251 24.007 139.241 1.00109.34 O ANISOU 1825 O LYS A1019 14975 15584 10984 -3391 415 -20 O ATOM 1826 CB LYS A1019 234.645 25.439 141.420 1.00104.73 C ANISOU 1826 CB LYS A1019 13884 16020 9890 -3589 625 -616 C ATOM 1827 CG LYS A1019 235.436 26.720 141.606 1.00105.17 C ANISOU 1827 CG LYS A1019 13943 15884 10132 -3259 609 -761 C ATOM 1828 CD LYS A1019 235.739 26.952 143.077 1.00103.72 C ANISOU 1828 CD LYS A1019 13717 15958 9735 -3471 623 -815 C ATOM 1829 CE LYS A1019 236.494 28.251 143.294 1.00104.90 C ANISOU 1829 CE LYS A1019 13872 15925 10059 -3153 599 -970 C ATOM 1830 NZ LYS A1019 236.787 28.485 144.735 1.00104.85 N ANISOU 1830 NZ LYS A1019 13818 16178 9843 -3356 616 -1030 N ATOM 1831 N ASP A1020 235.742 25.970 138.246 1.00109.99 N ANISOU 1831 N ASP A1020 14825 15645 11319 -2805 510 -443 N ATOM 1832 CA ASP A1020 236.919 25.971 137.391 1.00109.49 C ANISOU 1832 CA ASP A1020 14974 15089 11537 -2610 422 -244 C ATOM 1833 C ASP A1020 238.181 26.154 138.232 1.00113.97 C ANISOU 1833 C ASP A1020 15677 15500 12126 -2657 360 -127 C ATOM 1834 O ASP A1020 238.133 26.573 139.392 1.00117.45 O ANISOU 1834 O ASP A1020 16040 16182 12403 -2767 390 -240 O ATOM 1835 CB ASP A1020 236.811 27.080 136.341 1.00106.60 C ANISOU 1835 CB ASP A1020 14559 14547 11397 -2228 427 -420 C ATOM 1836 CG ASP A1020 237.750 26.874 135.168 1.00106.97 C ANISOU 1836 CG ASP A1020 14789 14154 11699 -2073 354 -216 C ATOM 1837 OD1 ASP A1020 238.851 26.320 135.368 1.00108.94 O ANISOU 1837 OD1 ASP A1020 15200 14196 11996 -2168 288 4 O ATOM 1838 OD2 ASP A1020 237.385 27.270 134.041 1.00106.80 O ANISOU 1838 OD2 ASP A1020 14744 14012 11825 -1857 355 -291 O ATOM 1839 N THR A1021 239.326 25.825 137.627 1.00114.67 N ANISOU 1839 N THR A1021 15958 15199 12413 -2571 270 87 N ATOM 1840 CA THR A1021 240.601 25.977 138.324 1.00114.20 C ANISOU 1840 CA THR A1021 16025 14976 12390 -2596 200 197 C ATOM 1841 C THR A1021 240.860 27.434 138.686 1.00113.31 C ANISOU 1841 C THR A1021 15839 14885 12328 -2396 237 -11 C ATOM 1842 O THR A1021 241.388 27.731 139.764 1.00112.51 O ANISOU 1842 O THR A1021 15754 14858 12137 -2488 225 -21 O ATOM 1843 CB THR A1021 241.744 25.430 137.467 1.00114.36 C ANISOU 1843 CB THR A1021 16224 14610 12619 -2499 97 412 C ATOM 1844 OG1 THR A1021 242.126 26.409 136.491 1.00109.33 O ANISOU 1844 OG1 THR A1021 15575 13773 12192 -2205 112 323 O ATOM 1845 CG2 THR A1021 241.317 24.154 136.755 1.00118.22 C ANISOU 1845 CG2 THR A1021 16774 15038 13107 -2606 50 564 C ATOM 1846 N GLU A1022 240.489 28.356 137.800 1.00111.96 N ANISOU 1846 N GLU A1022 15604 14639 12298 -2127 260 -178 N ATOM 1847 CA GLU A1022 240.646 29.780 138.059 1.00113.63 C ANISOU 1847 CA GLU A1022 15772 14839 12562 -1923 256 -389 C ATOM 1848 C GLU A1022 239.545 30.346 138.948 1.00115.72 C ANISOU 1848 C GLU A1022 15836 15493 12637 -1942 319 -676 C ATOM 1849 O GLU A1022 239.564 31.548 139.236 1.00116.89 O ANISOU 1849 O GLU A1022 15942 15651 12818 -1758 294 -891 O ATOM 1850 CB GLU A1022 240.691 30.548 136.735 1.00115.25 C ANISOU 1850 CB GLU A1022 16022 14782 12984 -1641 214 -447 C ATOM 1851 CG GLU A1022 241.725 30.019 135.753 1.00116.89 C ANISOU 1851 CG GLU A1022 16390 14659 13364 -1621 161 -199 C ATOM 1852 CD GLU A1022 241.684 30.738 134.419 1.00119.19 C ANISOU 1852 CD GLU A1022 16723 14729 13835 -1391 121 -249 C ATOM 1853 OE1 GLU A1022 241.370 31.947 134.402 1.00119.37 O ANISOU 1853 OE1 GLU A1022 16726 14741 13888 -1221 85 -447 O ATOM 1854 OE2 GLU A1022 241.965 30.092 133.387 1.00120.02 O ANISOU 1854 OE2 GLU A1022 16889 14668 14045 -1383 108 -95 O ATOM 1855 N GLY A1023 238.595 29.520 139.383 1.00116.64 N ANISOU 1855 N GLY A1023 15827 15944 12547 -2165 388 -699 N ATOM 1856 CA GLY A1023 237.554 29.968 140.285 1.00117.18 C ANISOU 1856 CA GLY A1023 15668 16460 12396 -2219 457 -993 C ATOM 1857 C GLY A1023 236.258 30.387 139.632 1.00115.81 C ANISOU 1857 C GLY A1023 15302 16483 12218 -2036 494 -1267 C ATOM 1858 O GLY A1023 235.490 31.140 140.243 1.00116.04 O ANISOU 1858 O GLY A1023 15125 16844 12120 -1956 522 -1597 O ATOM 1859 N TYR A1024 235.984 29.929 138.416 1.00113.72 N ANISOU 1859 N TYR A1024 15087 16037 12084 -1957 485 -1162 N ATOM 1860 CA TYR A1024 234.780 30.293 137.682 1.00113.36 C ANISOU 1860 CA TYR A1024 14873 16146 12053 -1768 505 -1410 C ATOM 1861 C TYR A1024 233.840 29.096 137.594 1.00111.90 C ANISOU 1861 C TYR A1024 14578 16256 11683 -2034 590 -1346 C ATOM 1862 O TYR A1024 234.192 27.968 137.947 1.00112.98 O ANISOU 1862 O TYR A1024 14817 16398 11712 -2352 605 -1075 O ATOM 1863 CB TYR A1024 235.134 30.806 136.280 1.00115.85 C ANISOU 1863 CB TYR A1024 15332 16028 12659 -1464 419 -1357 C ATOM 1864 CG TYR A1024 236.091 31.982 136.273 1.00117.50 C ANISOU 1864 CG TYR A1024 15682 15925 13039 -1239 315 -1394 C ATOM 1865 CD1 TYR A1024 236.167 32.851 137.356 1.00120.93 C ANISOU 1865 CD1 TYR A1024 16045 16519 13384 -1191 294 -1608 C ATOM 1866 CD2 TYR A1024 236.925 32.216 135.187 1.00115.99 C ANISOU 1866 CD2 TYR A1024 15693 15296 13080 -1096 234 -1215 C ATOM 1867 CE1 TYR A1024 237.040 33.921 137.355 1.00121.89 C ANISOU 1867 CE1 TYR A1024 16315 16346 13653 -1006 184 -1633 C ATOM 1868 CE2 TYR A1024 237.803 33.285 135.177 1.00116.39 C ANISOU 1868 CE2 TYR A1024 15886 15078 13261 -936 131 -1236 C ATOM 1869 CZ TYR A1024 237.856 34.134 136.264 1.00119.57 C ANISOU 1869 CZ TYR A1024 16234 15618 13578 -892 101 -1439 C ATOM 1870 OH TYR A1024 238.727 35.201 136.262 1.00121.35 O ANISOU 1870 OH TYR A1024 16619 15566 13924 -751 -17 -1452 O ATOM 1871 N TYR A1025 232.627 29.356 137.115 1.00109.13 N ANISOU 1871 N TYR A1025 14027 16148 11291 -1904 624 -1603 N ATOM 1872 CA TYR A1025 231.608 28.320 136.981 1.00107.45 C ANISOU 1872 CA TYR A1025 13684 16257 10886 -2152 707 -1581 C ATOM 1873 C TYR A1025 231.653 27.727 135.578 1.00104.53 C ANISOU 1873 C TYR A1025 13454 15549 10712 -2070 677 -1369 C ATOM 1874 O TYR A1025 231.480 28.444 134.586 1.00103.37 O ANISOU 1874 O TYR A1025 13308 15199 10770 -1740 630 -1489 O ATOM 1875 CB TYR A1025 230.219 28.883 137.278 1.00111.08 C ANISOU 1875 CB TYR A1025 13809 17233 11162 -2070 767 -2008 C ATOM 1876 CG TYR A1025 229.954 29.133 138.746 1.00112.64 C ANISOU 1876 CG TYR A1025 13814 17909 11076 -2260 826 -2221 C ATOM 1877 CD1 TYR A1025 229.849 28.076 139.640 1.00113.91 C ANISOU 1877 CD1 TYR A1025 13953 18387 10942 -2736 901 -2055 C ATOM 1878 CD2 TYR A1025 229.796 30.424 139.236 1.00115.20 C ANISOU 1878 CD2 TYR A1025 13986 18371 11416 -1974 787 -2594 C ATOM 1879 CE1 TYR A1025 229.603 28.296 140.982 1.00116.70 C ANISOU 1879 CE1 TYR A1025 14121 19207 11012 -2942 958 -2248 C ATOM 1880 CE2 TYR A1025 229.548 30.654 140.578 1.00117.73 C ANISOU 1880 CE2 TYR A1025 14109 19157 11467 -2146 844 -2811 C ATOM 1881 CZ TYR A1025 229.452 29.585 141.445 1.00119.95 C ANISOU 1881 CZ TYR A1025 14355 19776 11446 -2640 940 -2635 C ATOM 1882 OH TYR A1025 229.205 29.807 142.780 1.00122.51 O ANISOU 1882 OH TYR A1025 14476 20592 11479 -2841 1000 -2849 O ATOM 1883 N THR A1026 231.884 26.419 135.501 1.00102.42 N ANISOU 1883 N THR A1026 13317 15218 10378 -2374 686 -1058 N ATOM 1884 CA THR A1026 231.882 25.678 134.250 1.00101.73 C ANISOU 1884 CA THR A1026 13353 14857 10444 -2341 659 -855 C ATOM 1885 C THR A1026 230.992 24.452 134.404 1.00101.20 C ANISOU 1885 C THR A1026 13219 15099 10134 -2698 712 -769 C ATOM 1886 O THR A1026 230.545 24.106 135.501 1.00103.56 O ANISOU 1886 O THR A1026 13411 15793 10142 -3012 759 -818 O ATOM 1887 CB THR A1026 233.300 25.259 133.828 1.00101.41 C ANISOU 1887 CB THR A1026 13598 14320 10614 -2319 567 -529 C ATOM 1888 OG1 THR A1026 233.906 24.495 134.876 1.00103.28 O ANISOU 1888 OG1 THR A1026 13946 14598 10698 -2634 538 -333 O ATOM 1889 CG2 THR A1026 234.163 26.483 133.540 1.00100.00 C ANISOU 1889 CG2 THR A1026 13489 13842 10664 -1992 514 -605 C ATOM 1890 N ILE A1027 230.731 23.798 133.273 1.00 97.27 N ANISOU 1890 N ILE A1027 12789 14425 9745 -2668 696 -639 N ATOM 1891 CA ILE A1027 229.867 22.623 133.230 1.00 91.76 C ANISOU 1891 CA ILE A1027 12054 13975 8836 -2998 728 -543 C ATOM 1892 C ILE A1027 230.133 21.933 131.901 1.00 91.23 C ANISOU 1892 C ILE A1027 12160 13519 8986 -2902 667 -323 C ATOM 1893 O ILE A1027 230.584 22.560 130.945 1.00 90.98 O ANISOU 1893 O ILE A1027 12179 13163 9226 -2559 639 -346 O ATOM 1894 CB ILE A1027 228.374 23.012 133.398 1.00 91.81 C ANISOU 1894 CB ILE A1027 11732 14523 8628 -3017 840 -885 C ATOM 1895 CG1 ILE A1027 227.507 21.786 133.720 1.00 93.85 C ANISOU 1895 CG1 ILE A1027 11941 15143 8575 -3475 879 -785 C ATOM 1896 CG2 ILE A1027 227.867 23.706 132.148 1.00 92.15 C ANISOU 1896 CG2 ILE A1027 11680 14443 8891 -2622 848 -1069 C ATOM 1897 CD1 ILE A1027 226.072 22.146 134.080 1.00100.15 C ANISOU 1897 CD1 ILE A1027 12377 16573 9104 -3549 999 -1147 C ATOM 1898 N GLY A1028 229.889 20.626 131.857 1.00 91.34 N ANISOU 1898 N GLY A1028 12279 13560 8867 -3225 630 -104 N ATOM 1899 CA GLY A1028 230.111 19.869 130.648 1.00 92.17 C ANISOU 1899 CA GLY A1028 12546 13319 9157 -3155 561 96 C ATOM 1900 C GLY A1028 231.587 19.658 130.381 1.00 93.43 C ANISOU 1900 C GLY A1028 12961 12987 9550 -3031 437 325 C ATOM 1901 O GLY A1028 232.364 19.227 131.248 1.00 96.97 O ANISOU 1901 O GLY A1028 13560 13355 9928 -3218 351 482 O ATOM 1902 N ILE A1029 231.965 19.991 129.146 1.00 90.82 N ANISOU 1902 N ILE A1029 12669 12346 9492 -2713 423 327 N ATOM 1903 CA ILE A1029 233.298 19.775 128.590 1.00 89.27 C ANISOU 1903 CA ILE A1029 12676 11711 9531 -2563 313 511 C ATOM 1904 C ILE A1029 234.105 21.072 128.671 1.00 98.08 C ANISOU 1904 C ILE A1029 13766 12699 10801 -2291 333 395 C ATOM 1905 O ILE A1029 234.924 21.366 127.817 1.00103.51 O ANISOU 1905 O ILE A1029 14533 13087 11708 -2070 291 443 O ATOM 1906 CB ILE A1029 233.196 19.292 127.141 1.00 86.54 C ANISOU 1906 CB ILE A1029 12377 11143 9359 -2422 286 583 C ATOM 1907 CG1 ILE A1029 232.182 18.144 127.048 1.00 88.16 C ANISOU 1907 CG1 ILE A1029 12584 11518 9392 -2692 277 661 C ATOM 1908 CG2 ILE A1029 234.517 18.709 126.667 1.00 80.61 C ANISOU 1908 CG2 ILE A1029 11830 10005 8793 -2345 152 778 C ATOM 1909 CD1 ILE A1029 232.572 16.916 127.746 1.00 92.23 C ANISOU 1909 CD1 ILE A1029 13298 11967 9777 -3005 139 886 C ATOM 1910 N GLY A1030 233.831 21.881 129.689 1.00 98.44 N ANISOU 1910 N GLY A1030 13692 12996 10714 -2319 395 227 N ATOM 1911 CA GLY A1030 234.645 23.056 129.956 1.00 98.72 C ANISOU 1911 CA GLY A1030 13734 12909 10867 -2107 389 133 C ATOM 1912 C GLY A1030 233.987 24.319 129.446 1.00 99.25 C ANISOU 1912 C GLY A1030 13650 13050 11010 -1833 445 -129 C ATOM 1913 O GLY A1030 234.617 25.315 129.064 1.00100.28 O ANISOU 1913 O GLY A1030 13826 12968 11308 -1594 409 -187 O ATOM 1914 N HIS A1031 232.669 24.242 129.443 1.00 97.71 N ANISOU 1914 N HIS A1031 13281 13171 10675 -1883 515 -292 N ATOM 1915 CA HIS A1031 231.808 25.316 128.987 1.00 98.64 C ANISOU 1915 CA HIS A1031 13235 13408 10838 -1624 544 -577 C ATOM 1916 C HIS A1031 231.783 26.404 130.050 1.00 99.54 C ANISOU 1916 C HIS A1031 13243 13710 10867 -1546 549 -813 C ATOM 1917 O HIS A1031 231.054 26.308 131.039 1.00100.55 O ANISOU 1917 O HIS A1031 13203 14241 10762 -1713 612 -965 O ATOM 1918 CB HIS A1031 230.421 24.768 128.712 1.00 98.05 C ANISOU 1918 CB HIS A1031 12987 13652 10616 -1723 613 -686 C ATOM 1919 CG HIS A1031 229.498 25.777 128.130 1.00101.13 C ANISOU 1919 CG HIS A1031 13210 14152 11064 -1433 618 -988 C ATOM 1920 ND1 HIS A1031 229.465 26.051 126.781 1.00101.57 N ANISOU 1920 ND1 HIS A1031 13329 13932 11329 -1195 569 -971 N ATOM 1921 CD2 HIS A1031 228.595 26.602 128.707 1.00103.44 C ANISOU 1921 CD2 HIS A1031 13276 14794 11231 -1327 642 -1331 C ATOM 1922 CE1 HIS A1031 228.573 26.996 126.550 1.00103.64 C ANISOU 1922 CE1 HIS A1031 13434 14345 11601 -954 549 -1277 C ATOM 1923 NE2 HIS A1031 228.028 27.345 127.702 1.00104.56 N ANISOU 1923 NE2 HIS A1031 13365 14844 11520 -1013 590 -1514 N ATOM 1924 N LEU A1032 232.620 27.423 129.866 1.00100.10 N ANISOU 1924 N LEU A1032 13418 13499 11115 -1314 475 -841 N ATOM 1925 CA LEU A1032 232.690 28.545 130.791 1.00100.15 C ANISOU 1925 CA LEU A1032 13355 13624 11072 -1203 451 -1068 C ATOM 1926 C LEU A1032 231.346 29.258 130.862 1.00101.95 C ANISOU 1926 C LEU A1032 13347 14179 11211 -1038 463 -1438 C ATOM 1927 O LEU A1032 230.908 29.873 129.886 1.00102.04 O ANISOU 1927 O LEU A1032 13350 14058 11363 -776 398 -1566 O ATOM 1928 CB LEU A1032 233.797 29.510 130.367 1.00100.61 C ANISOU 1928 CB LEU A1032 13597 13284 11348 -986 346 -1016 C ATOM 1929 CG LEU A1032 234.020 30.723 131.268 1.00101.90 C ANISOU 1929 CG LEU A1032 13734 13497 11486 -858 291 -1230 C ATOM 1930 CD1 LEU A1032 234.462 30.283 132.653 1.00104.31 C ANISOU 1930 CD1 LEU A1032 14015 14002 11617 -1110 352 -1165 C ATOM 1931 CD2 LEU A1032 235.036 31.673 130.653 1.00100.87 C ANISOU 1931 CD2 LEU A1032 13808 12953 11564 -665 168 -1164 C ATOM 1932 N LEU A1033 230.684 29.178 132.015 1.00105.26 N ANISOU 1932 N LEU A1033 13566 15044 11386 -1193 535 -1625 N ATOM 1933 CA LEU A1033 229.357 29.765 132.152 1.00111.89 C ANISOU 1933 CA LEU A1033 14132 16273 12107 -1045 550 -2020 C ATOM 1934 C LEU A1033 229.437 31.266 132.410 1.00113.74 C ANISOU 1934 C LEU A1033 14339 16440 12436 -706 432 -2324 C ATOM 1935 O LEU A1033 228.936 32.071 131.618 1.00115.68 O ANISOU 1935 O LEU A1033 14562 16571 12818 -385 327 -2531 O ATOM 1936 CB LEU A1033 228.588 29.062 133.273 1.00116.01 C ANISOU 1936 CB LEU A1033 14425 17358 12295 -1376 675 -2121 C ATOM 1937 CG LEU A1033 228.301 27.578 133.038 1.00116.80 C ANISOU 1937 CG LEU A1033 14551 17562 12265 -1733 762 -1852 C ATOM 1938 CD1 LEU A1033 227.741 26.927 134.292 1.00117.99 C ANISOU 1938 CD1 LEU A1033 14526 18248 12056 -2130 862 -1908 C ATOM 1939 CD2 LEU A1033 227.350 27.401 131.865 1.00113.63 C ANISOU 1939 CD2 LEU A1033 14058 17188 11927 -1598 770 -1936 C ATOM 1940 N THR A1034 230.066 31.659 133.515 1.00113.24 N ANISOU 1940 N THR A1034 14295 16430 12300 -773 428 -2354 N ATOM 1941 CA THR A1034 230.165 33.067 133.871 1.00116.12 C ANISOU 1941 CA THR A1034 14646 16734 12740 -468 299 -2648 C ATOM 1942 C THR A1034 231.284 33.253 134.884 1.00113.75 C ANISOU 1942 C THR A1034 14470 16338 12412 -600 300 -2517 C ATOM 1943 O THR A1034 231.592 32.349 135.664 1.00115.13 O ANISOU 1943 O THR A1034 14630 16693 12422 -936 415 -2330 O ATOM 1944 CB THR A1034 228.846 33.602 134.442 1.00122.27 C ANISOU 1944 CB THR A1034 15093 18025 13339 -331 301 -3130 C ATOM 1945 OG1 THR A1034 229.007 34.975 134.821 1.00125.97 O ANISOU 1945 OG1 THR A1034 15573 18398 13890 -15 141 -3424 O ATOM 1946 CG2 THR A1034 228.418 32.790 135.656 1.00124.56 C ANISOU 1946 CG2 THR A1034 15155 18869 13303 -699 471 -3172 C ATOM 1947 N LYS A1035 231.892 34.437 134.854 1.00110.97 N ANISOU 1947 N LYS A1035 14255 15689 12219 -342 151 -2612 N ATOM 1948 CA LYS A1035 232.859 34.827 135.869 1.00108.69 C ANISOU 1948 CA LYS A1035 14058 15338 11900 -421 135 -2560 C ATOM 1949 C LYS A1035 232.203 35.458 137.088 1.00108.84 C ANISOU 1949 C LYS A1035 13834 15794 11728 -367 138 -2954 C ATOM 1950 O LYS A1035 232.894 35.717 138.080 1.00111.98 O ANISOU 1950 O LYS A1035 14269 16218 12060 -463 144 -2936 O ATOM 1951 CB LYS A1035 233.887 35.801 135.281 1.00105.85 C ANISOU 1951 CB LYS A1035 13978 14455 11783 -208 -34 -2461 C ATOM 1952 CG LYS A1035 234.768 35.199 134.199 1.00104.38 C ANISOU 1952 CG LYS A1035 14029 13866 11765 -298 -29 -2065 C ATOM 1953 CD LYS A1035 235.799 36.204 133.711 1.00102.68 C ANISOU 1953 CD LYS A1035 14075 13197 11742 -141 -194 -1979 C ATOM 1954 CE LYS A1035 236.695 35.604 132.641 1.00101.59 C ANISOU 1954 CE LYS A1035 14135 12719 11744 -247 -181 -1614 C ATOM 1955 NZ LYS A1035 237.715 36.577 132.162 1.00 99.98 N ANISOU 1955 NZ LYS A1035 14179 12119 11691 -147 -336 -1526 N ATOM 1956 N SER A1036 230.901 35.714 137.038 1.00107.43 N ANISOU 1956 N SER A1036 13394 15974 11452 -211 131 -3326 N ATOM 1957 CA SER A1036 230.203 36.259 138.193 1.00107.49 C ANISOU 1957 CA SER A1036 13120 16472 11251 -159 140 -3748 C ATOM 1958 C SER A1036 230.192 35.228 139.316 1.00104.49 C ANISOU 1958 C SER A1036 12590 16533 10578 -603 341 -3629 C ATOM 1959 O SER A1036 229.892 34.054 139.068 1.00107.20 O ANISOU 1959 O SER A1036 12899 17021 10812 -892 471 -3409 O ATOM 1960 CB SER A1036 228.775 36.653 137.818 1.00110.77 C ANISOU 1960 CB SER A1036 13258 17217 11613 103 88 -4188 C ATOM 1961 OG SER A1036 228.064 37.139 138.943 1.00114.08 O ANISOU 1961 OG SER A1036 13362 18176 11809 153 101 -4638 O ATOM 1962 N PRO A1037 230.518 35.615 140.553 1.00100.54 N ANISOU 1962 N PRO A1037 12018 16246 9937 -684 356 -3759 N ATOM 1963 CA PRO A1037 230.548 34.637 141.650 1.00 98.76 C ANISOU 1963 CA PRO A1037 11679 16431 9415 -1142 527 -3624 C ATOM 1964 C PRO A1037 229.175 34.198 142.133 1.00103.28 C ANISOU 1964 C PRO A1037 11870 17705 9666 -1314 650 -3930 C ATOM 1965 O PRO A1037 229.101 33.352 143.032 1.00106.27 O ANISOU 1965 O PRO A1037 12153 18465 9760 -1743 784 -3818 O ATOM 1966 CB PRO A1037 231.307 35.386 142.754 1.00 98.84 C ANISOU 1966 CB PRO A1037 11728 16433 9394 -1121 482 -3712 C ATOM 1967 CG PRO A1037 231.008 36.821 142.493 1.00 99.54 C ANISOU 1967 CG PRO A1037 11770 16407 9644 -636 305 -4118 C ATOM 1968 CD PRO A1037 230.926 36.960 140.995 1.00100.24 C ANISOU 1968 CD PRO A1037 12031 16053 10005 -377 197 -4014 C ATOM 1969 N SER A1038 228.089 34.731 141.577 1.00106.86 N ANISOU 1969 N SER A1038 12104 18358 10139 -1013 598 -4314 N ATOM 1970 CA SER A1038 226.748 34.362 142.017 1.00111.78 C ANISOU 1970 CA SER A1038 12326 19707 10439 -1167 715 -4651 C ATOM 1971 C SER A1038 226.376 33.001 141.440 1.00110.93 C ANISOU 1971 C SER A1038 12241 19678 10229 -1522 843 -4331 C ATOM 1972 O SER A1038 226.381 32.813 140.218 1.00106.40 O ANISOU 1972 O SER A1038 11829 18715 9885 -1363 792 -4157 O ATOM 1973 CB SER A1038 225.734 35.424 141.597 1.00116.72 C ANISOU 1973 CB SER A1038 12704 20511 11132 -686 589 -5201 C ATOM 1974 OG SER A1038 224.416 35.044 141.956 1.00118.76 O ANISOU 1974 OG SER A1038 12544 21512 11069 -832 708 -5549 O ATOM 1975 N LEU A1039 226.054 32.051 142.322 1.00113.18 N ANISOU 1975 N LEU A1039 12378 20466 10158 -2019 996 -4250 N ATOM 1976 CA LEU A1039 225.668 30.719 141.867 1.00110.48 C ANISOU 1976 CA LEU A1039 12071 20220 9684 -2400 1097 -3947 C ATOM 1977 C LEU A1039 224.314 30.746 141.169 1.00106.47 C ANISOU 1977 C LEU A1039 11272 20075 9106 -2255 1126 -4273 C ATOM 1978 O LEU A1039 224.115 30.054 140.163 1.00 97.45 O ANISOU 1978 O LEU A1039 10245 18719 8062 -2299 1136 -4042 O ATOM 1979 CB LEU A1039 225.648 29.748 143.048 1.00108.49 C ANISOU 1979 CB LEU A1039 11758 20423 9042 -3001 1219 -3783 C ATOM 1980 CG LEU A1039 225.236 28.306 142.748 1.00106.86 C ANISOU 1980 CG LEU A1039 11610 20350 8643 -3471 1298 -3461 C ATOM 1981 CD1 LEU A1039 226.168 27.679 141.724 1.00101.63 C ANISOU 1981 CD1 LEU A1039 11365 18949 8303 -3426 1216 -2965 C ATOM 1982 CD2 LEU A1039 225.208 27.483 144.024 1.00111.57 C ANISOU 1982 CD2 LEU A1039 12157 21412 8823 -4079 1382 -3328 C ATOM 1983 N ASN A1040 223.370 31.537 141.687 1.00112.29 N ANISOU 1983 N ASN A1040 11620 21376 9669 -2070 1133 -4830 N ATOM 1984 CA ASN A1040 222.068 31.649 141.037 1.00115.84 C ANISOU 1984 CA ASN A1040 11764 22196 10054 -1887 1144 -5196 C ATOM 1985 C ASN A1040 222.189 32.284 139.659 1.00115.78 C ANISOU 1985 C ASN A1040 11945 21582 10463 -1365 983 -5195 C ATOM 1986 O ASN A1040 221.445 31.920 138.740 1.00116.92 O ANISOU 1986 O ASN A1040 12016 21773 10635 -1309 997 -5221 O ATOM 1987 CB ASN A1040 221.107 32.453 141.914 1.00117.86 C ANISOU 1987 CB ASN A1040 11549 23183 10048 -1746 1157 -5843 C ATOM 1988 CG ASN A1040 220.732 31.722 143.189 1.00117.85 C ANISOU 1988 CG ASN A1040 11293 23848 9636 -2317 1320 -5824 C ATOM 1989 OD1 ASN A1040 220.829 30.497 143.267 1.00115.62 O ANISOU 1989 OD1 ASN A1040 11134 23642 9155 -2845 1437 -5428 O ATOM 1990 ND2 ASN A1040 220.299 32.472 144.195 1.00119.88 N ANISOU 1990 ND2 ASN A1040 11200 24492 9858 -2208 1286 -6175 N ATOM 1991 N ALA A1041 223.118 33.229 139.493 1.00114.28 N ANISOU 1991 N ALA A1041 12009 20827 10585 -1003 824 -5158 N ATOM 1992 CA ALA A1041 223.347 33.812 138.176 1.00111.44 C ANISOU 1992 CA ALA A1041 11882 19853 10608 -564 655 -5101 C ATOM 1993 C ALA A1041 223.948 32.790 137.221 1.00110.18 C ANISOU 1993 C ALA A1041 12042 19219 10604 -780 705 -4540 C ATOM 1994 O ALA A1041 223.602 32.762 136.034 1.00106.95 O ANISOU 1994 O ALA A1041 11696 18566 10374 -578 646 -4506 O ATOM 1995 CB ALA A1041 224.251 35.039 138.292 1.00112.13 C ANISOU 1995 CB ALA A1041 12186 19463 10954 -196 463 -5168 C ATOM 1996 N ALA A1042 224.852 31.942 137.720 1.00108.76 N ANISOU 1996 N ALA A1042 12066 18902 10355 -1179 798 -4111 N ATOM 1997 CA ALA A1042 225.383 30.863 136.896 1.00104.18 C ANISOU 1997 CA ALA A1042 11763 17929 9891 -1400 837 -3610 C ATOM 1998 C ALA A1042 224.285 29.880 136.509 1.00101.11 C ANISOU 1998 C ALA A1042 11186 17929 9302 -1645 950 -3617 C ATOM 1999 O ALA A1042 224.230 29.420 135.363 1.00 96.40 O ANISOU 1999 O ALA A1042 10727 17028 8872 -1588 931 -3412 O ATOM 2000 CB ALA A1042 226.517 30.147 137.630 1.00 98.26 C ANISOU 2000 CB ALA A1042 11249 17003 9084 -1770 885 -3200 C ATOM 2001 N LYS A1043 223.399 29.550 137.454 1.00104.43 N ANISOU 2001 N LYS A1043 11285 19046 9348 -1937 1067 -3856 N ATOM 2002 CA LYS A1043 222.252 28.710 137.126 1.00107.42 C ANISOU 2002 CA LYS A1043 11448 19866 9499 -2177 1170 -3916 C ATOM 2003 C LYS A1043 221.295 29.422 136.181 1.00109.18 C ANISOU 2003 C LYS A1043 11470 20159 9856 -1734 1106 -4295 C ATOM 2004 O LYS A1043 220.620 28.769 135.375 1.00110.99 O ANISOU 2004 O LYS A1043 11650 20461 10060 -1813 1150 -4231 O ATOM 2005 CB LYS A1043 221.519 28.290 138.400 1.00105.09 C ANISOU 2005 CB LYS A1043 10833 20359 8738 -2613 1305 -4120 C ATOM 2006 CG LYS A1043 222.301 27.340 139.290 1.00106.08 C ANISOU 2006 CG LYS A1043 11168 20462 8676 -3146 1361 -3705 C ATOM 2007 CD LYS A1043 221.476 26.924 140.496 1.00106.83 C ANISOU 2007 CD LYS A1043 10937 21384 8271 -3620 1489 -3914 C ATOM 2008 CE LYS A1043 222.224 25.930 141.366 1.00108.88 C ANISOU 2008 CE LYS A1043 11440 21602 8329 -4183 1512 -3478 C ATOM 2009 NZ LYS A1043 221.419 25.522 142.550 1.00112.17 N ANISOU 2009 NZ LYS A1043 11549 22847 8224 -4700 1631 -3667 N ATOM 2010 N SER A1044 221.223 30.751 136.263 1.00111.97 N ANISOU 2010 N SER A1044 11717 20476 10352 -1264 982 -4692 N ATOM 2011 CA SER A1044 220.364 31.503 135.355 1.00110.95 C ANISOU 2011 CA SER A1044 11430 20354 10372 -801 869 -5062 C ATOM 2012 C SER A1044 220.859 31.387 133.917 1.00107.97 C ANISOU 2012 C SER A1044 11393 19281 10351 -602 774 -4723 C ATOM 2013 O SER A1044 220.092 31.041 133.011 1.00103.57 O ANISOU 2013 O SER A1044 10753 18784 9814 -545 785 -4760 O ATOM 2014 CB SER A1044 220.295 32.966 135.793 1.00116.36 C ANISOU 2014 CB SER A1044 11988 21078 11147 -333 704 -5543 C ATOM 2015 OG SER A1044 219.793 33.080 137.114 1.00118.28 O ANISOU 2015 OG SER A1044 11880 22016 11046 -509 797 -5897 O ATOM 2016 N GLU A1045 222.145 31.662 133.692 1.00109.23 N ANISOU 2016 N GLU A1045 11925 18799 10777 -513 684 -4393 N ATOM 2017 CA GLU A1045 222.707 31.561 132.350 1.00110.36 C ANISOU 2017 CA GLU A1045 12389 18305 11239 -355 598 -4067 C ATOM 2018 C GLU A1045 222.805 30.123 131.865 1.00112.07 C ANISOU 2018 C GLU A1045 12721 18463 11398 -745 734 -3641 C ATOM 2019 O GLU A1045 222.855 29.896 130.651 1.00111.33 O ANISOU 2019 O GLU A1045 12784 18008 11506 -628 690 -3457 O ATOM 2020 CB GLU A1045 224.097 32.193 132.303 1.00113.64 C ANISOU 2020 CB GLU A1045 13151 18115 11913 -209 476 -3832 C ATOM 2021 CG GLU A1045 224.107 33.700 132.162 1.00116.00 C ANISOU 2021 CG GLU A1045 13474 18204 12397 273 258 -4170 C ATOM 2022 CD GLU A1045 225.514 34.250 132.039 1.00117.83 C ANISOU 2022 CD GLU A1045 14071 17833 12865 358 141 -3894 C ATOM 2023 OE1 GLU A1045 226.475 33.461 132.165 1.00112.36 O ANISOU 2023 OE1 GLU A1045 13571 16939 12180 53 244 -3476 O ATOM 2024 OE2 GLU A1045 225.660 35.471 131.819 1.00123.54 O ANISOU 2024 OE2 GLU A1045 14893 18288 13760 725 -70 -4102 O ATOM 2025 N LEU A1046 222.836 29.152 132.780 1.00111.20 N ANISOU 2025 N LEU A1046 12549 18690 11011 -1209 879 -3480 N ATOM 2026 CA LEU A1046 223.062 27.761 132.408 1.00109.62 C ANISOU 2026 CA LEU A1046 12517 18375 10761 -1594 965 -3048 C ATOM 2027 C LEU A1046 221.953 27.208 131.524 1.00107.49 C ANISOU 2027 C LEU A1046 12095 18313 10431 -1618 1013 -3119 C ATOM 2028 O LEU A1046 222.146 26.163 130.895 1.00104.87 O ANISOU 2028 O LEU A1046 11942 17770 10134 -1840 1044 -2766 O ATOM 2029 CB LEU A1046 223.212 26.914 133.680 1.00107.73 C ANISOU 2029 CB LEU A1046 12242 18493 10199 -2101 1072 -2904 C ATOM 2030 CG LEU A1046 223.556 25.416 133.657 1.00106.34 C ANISOU 2030 CG LEU A1046 12273 18219 9912 -2575 1122 -2447 C ATOM 2031 CD1 LEU A1046 222.317 24.524 133.603 1.00110.26 C ANISOU 2031 CD1 LEU A1046 12554 19229 10110 -2904 1221 -2512 C ATOM 2032 CD2 LEU A1046 224.533 25.079 132.535 1.00100.68 C ANISOU 2032 CD2 LEU A1046 11910 16807 9537 -2431 1035 -2069 C ATOM 2033 N ASP A1047 220.813 27.892 131.430 1.00110.94 N ANISOU 2033 N ASP A1047 12213 19149 10791 -1374 1004 -3579 N ATOM 2034 CA ASP A1047 219.670 27.351 130.717 1.00114.84 C ANISOU 2034 CA ASP A1047 12517 19935 11181 -1427 1062 -3683 C ATOM 2035 C ASP A1047 219.113 28.265 129.635 1.00115.28 C ANISOU 2035 C ASP A1047 12503 19824 11475 -913 937 -3968 C ATOM 2036 O ASP A1047 218.134 27.889 128.980 1.00114.81 O ANISOU 2036 O ASP A1047 12275 20001 11346 -916 976 -4081 O ATOM 2037 CB ASP A1047 218.561 26.993 131.711 1.00116.88 C ANISOU 2037 CB ASP A1047 12382 21021 11008 -1747 1196 -3985 C ATOM 2038 CG ASP A1047 218.893 25.754 132.519 1.00115.53 C ANISOU 2038 CG ASP A1047 12309 21024 10562 -2358 1312 -3629 C ATOM 2039 OD1 ASP A1047 219.596 24.872 131.984 1.00109.97 O ANISOU 2039 OD1 ASP A1047 11935 19864 9986 -2545 1298 -3162 O ATOM 2040 OD2 ASP A1047 218.464 25.668 133.689 1.00118.55 O ANISOU 2040 OD2 ASP A1047 12449 21998 10597 -2652 1400 -3823 O ATOM 2041 N LYS A1048 219.699 29.446 129.423 1.00117.19 N ANISOU 2041 N LYS A1048 12884 19660 11985 -489 772 -4082 N ATOM 2042 CA LYS A1048 219.371 30.214 128.228 1.00115.68 C ANISOU 2042 CA LYS A1048 12739 19157 12057 -34 612 -4240 C ATOM 2043 C LYS A1048 219.768 29.463 126.965 1.00119.08 C ANISOU 2043 C LYS A1048 13441 19120 12682 -108 621 -3816 C ATOM 2044 O LYS A1048 219.221 29.737 125.890 1.00121.65 O ANISOU 2044 O LYS A1048 13757 19311 13153 156 534 -3919 O ATOM 2045 CB LYS A1048 220.047 31.588 128.273 1.00113.65 C ANISOU 2045 CB LYS A1048 12644 18501 12038 378 403 -4386 C ATOM 2046 CG LYS A1048 219.187 32.689 128.888 1.00112.40 C ANISOU 2046 CG LYS A1048 12176 18746 11785 711 288 -4984 C ATOM 2047 CD LYS A1048 218.856 32.393 130.343 1.00114.78 C ANISOU 2047 CD LYS A1048 12175 19698 11739 419 446 -5186 C ATOM 2048 CE LYS A1048 218.026 33.500 130.972 1.00117.76 C ANISOU 2048 CE LYS A1048 12219 20508 12018 773 324 -5822 C ATOM 2049 NZ LYS A1048 217.675 33.186 132.387 1.00120.26 N ANISOU 2049 NZ LYS A1048 12210 21520 11963 456 492 -6034 N ATOM 2050 N ALA A1049 220.698 28.512 127.080 1.00117.34 N ANISOU 2050 N ALA A1049 13458 18663 12464 -456 713 -3358 N ATOM 2051 CA ALA A1049 221.083 27.649 125.974 1.00113.18 C ANISOU 2051 CA ALA A1049 13164 17750 12088 -566 732 -2965 C ATOM 2052 C ALA A1049 220.503 26.243 126.075 1.00113.92 C ANISOU 2052 C ALA A1049 13162 18180 11941 -997 887 -2799 C ATOM 2053 O ALA A1049 220.352 25.580 125.043 1.00118.02 O ANISOU 2053 O ALA A1049 13777 18513 12552 -1034 898 -2603 O ATOM 2054 CB ALA A1049 222.611 27.555 125.883 1.00109.61 C ANISOU 2054 CB ALA A1049 13071 16741 11837 -616 687 -2571 C ATOM 2055 N ILE A1050 220.170 25.776 127.276 1.00110.08 N ANISOU 2055 N ILE A1050 12500 18185 11139 -1339 995 -2870 N ATOM 2056 CA ILE A1050 219.708 24.400 127.448 1.00109.16 C ANISOU 2056 CA ILE A1050 12344 18363 10767 -1815 1114 -2669 C ATOM 2057 C ILE A1050 218.203 24.282 127.236 1.00111.89 C ANISOU 2057 C ILE A1050 12342 19271 10899 -1842 1186 -2994 C ATOM 2058 O ILE A1050 217.738 23.357 126.565 1.00114.13 O ANISOU 2058 O ILE A1050 12648 19585 11131 -2038 1233 -2828 O ATOM 2059 CB ILE A1050 220.135 23.871 128.831 1.00106.32 C ANISOU 2059 CB ILE A1050 12004 18246 10146 -2237 1178 -2540 C ATOM 2060 CG1 ILE A1050 221.660 23.760 128.900 1.00 99.90 C ANISOU 2060 CG1 ILE A1050 11561 16846 9552 -2240 1103 -2166 C ATOM 2061 CG2 ILE A1050 219.490 22.526 129.116 1.00110.74 C ANISOU 2061 CG2 ILE A1050 12507 19186 10384 -2766 1275 -2379 C ATOM 2062 CD1 ILE A1050 222.266 22.957 127.766 1.00 95.76 C ANISOU 2062 CD1 ILE A1050 11332 15800 9252 -2253 1054 -1780 C ATOM 2063 N GLY A1051 217.417 25.200 127.795 1.00113.34 N ANISOU 2063 N GLY A1051 12192 19919 10951 -1642 1187 -3475 N ATOM 2064 CA GLY A1051 215.999 25.259 127.509 1.00114.09 C ANISOU 2064 CA GLY A1051 11928 20547 10873 -1581 1232 -3849 C ATOM 2065 C GLY A1051 215.092 24.645 128.553 1.00115.69 C ANISOU 2065 C GLY A1051 11800 21543 10614 -2031 1381 -4032 C ATOM 2066 O GLY A1051 213.874 24.605 128.337 1.00122.58 O ANISOU 2066 O GLY A1051 12343 22928 11303 -2026 1434 -4352 O ATOM 2067 N ARG A1052 215.634 24.157 129.662 1.00112.29 N ANISOU 2067 N ARG A1052 11444 21248 9974 -2439 1445 -3843 N ATOM 2068 CA ARG A1052 214.839 23.671 130.779 1.00114.62 C ANISOU 2068 CA ARG A1052 11428 22329 9795 -2904 1577 -4025 C ATOM 2069 C ARG A1052 215.172 24.483 132.025 1.00111.03 C ANISOU 2069 C ARG A1052 10839 22117 9231 -2851 1574 -4276 C ATOM 2070 O ARG A1052 215.935 25.448 131.974 1.00107.51 O ANISOU 2070 O ARG A1052 10532 21236 9082 -2431 1463 -4330 O ATOM 2071 CB ARG A1052 215.076 22.176 131.014 1.00121.54 C ANISOU 2071 CB ARG A1052 12527 23201 10453 -3543 1643 -3545 C ATOM 2072 CG ARG A1052 214.610 21.285 129.869 1.00122.74 C ANISOU 2072 CG ARG A1052 12776 23205 10654 -3651 1651 -3328 C ATOM 2073 CD ARG A1052 214.910 19.816 130.133 1.00119.30 C ANISOU 2073 CD ARG A1052 12609 22708 10013 -4274 1668 -2847 C ATOM 2074 NE ARG A1052 216.333 19.572 130.351 1.00118.03 N ANISOU 2074 NE ARG A1052 12867 21916 10063 -4307 1571 -2434 N ATOM 2075 CZ ARG A1052 216.851 19.155 131.503 1.00118.88 C ANISOU 2075 CZ ARG A1052 13086 22134 9949 -4710 1567 -2258 C ATOM 2076 NH1 ARG A1052 216.060 18.926 132.543 1.00126.25 N ANISOU 2076 NH1 ARG A1052 13747 23795 10426 -5147 1662 -2445 N ATOM 2077 NH2 ARG A1052 218.157 18.956 131.616 1.00116.08 N ANISOU 2077 NH2 ARG A1052 13109 21184 9813 -4691 1464 -1901 N ATOM 2078 N ASN A1053 214.581 24.090 133.154 1.00114.93 N ANISOU 2078 N ASN A1053 11059 23333 9277 -3303 1692 -4434 N ATOM 2079 CA ASN A1053 214.911 24.712 134.430 1.00113.79 C ANISOU 2079 CA ASN A1053 10788 23462 8985 -3336 1703 -4639 C ATOM 2080 C ASN A1053 216.061 24.011 135.134 1.00116.38 C ANISOU 2080 C ASN A1053 11480 23469 9272 -3748 1704 -4145 C ATOM 2081 O ASN A1053 216.867 24.677 135.793 1.00120.29 O ANISOU 2081 O ASN A1053 12062 23771 9869 -3594 1655 -4169 O ATOM 2082 CB ASN A1053 213.682 24.739 135.341 1.00116.67 C ANISOU 2082 CB ASN A1053 10640 24526 9162 -3548 1709 -4939 C ATOM 2083 CG ASN A1053 212.718 25.854 134.984 1.00114.93 C ANISOU 2083 CG ASN A1053 10021 24545 9101 -2999 1625 -5487 C ATOM 2084 OD1 ASN A1053 213.091 26.825 134.330 1.00113.70 O ANISOU 2084 OD1 ASN A1053 9978 24014 9210 -2427 1533 -5679 O ATOM 2085 ND2 ASN A1053 211.477 25.736 135.446 1.00119.92 N ANISOU 2085 ND2 ASN A1053 10187 25802 9575 -3180 1625 -5746 N ATOM 2086 N THR A1054 216.144 22.683 135.017 1.00121.12 N ANISOU 2086 N THR A1054 12298 24002 9722 -4264 1738 -3707 N ATOM 2087 CA THR A1054 217.295 21.882 135.437 1.00118.59 C ANISOU 2087 CA THR A1054 12398 23236 9427 -4615 1686 -3179 C ATOM 2088 C THR A1054 217.607 21.949 136.931 1.00126.33 C ANISOU 2088 C THR A1054 13312 24580 10107 -4956 1722 -3217 C ATOM 2089 O THR A1054 217.702 20.904 137.584 1.00130.90 O ANISOU 2089 O THR A1054 14023 25254 10459 -5529 1706 -2894 O ATOM 2090 CB THR A1054 218.550 22.279 134.649 1.00112.28 C ANISOU 2090 CB THR A1054 11980 21544 9138 -4165 1558 -2911 C ATOM 2091 OG1 THR A1054 218.896 23.644 134.919 1.00109.95 O ANISOU 2091 OG1 THR A1054 11576 21166 9035 -3685 1519 -3230 O ATOM 2092 CG2 THR A1054 218.318 22.095 133.157 1.00114.38 C ANISOU 2092 CG2 THR A1054 12347 21429 9684 -3888 1518 -2819 C ATOM 2093 N ASN A1055 217.795 23.156 137.470 1.00119.86 N ANISOU 2093 N ASN A1055 12310 23861 9369 -4588 1718 -3573 N ATOM 2094 CA ASN A1055 218.283 23.351 138.837 1.00116.61 C ANISOU 2094 CA ASN A1055 11872 23657 8777 -4823 1726 -3584 C ATOM 2095 C ASN A1055 219.693 22.782 139.002 1.00118.65 C ANISOU 2095 C ASN A1055 12625 23273 9182 -4997 1639 -3049 C ATOM 2096 O ASN A1055 219.962 21.958 139.879 1.00119.01 O ANISOU 2096 O ASN A1055 12801 23475 8943 -5542 1644 -2785 O ATOM 2097 CB ASN A1055 217.325 22.752 139.873 1.00115.42 C ANISOU 2097 CB ASN A1055 11387 24102 8365 -5338 1740 -3629 C ATOM 2098 CG ASN A1055 217.581 23.274 141.274 1.00118.41 C ANISOU 2098 CG ASN A1055 11599 24758 8635 -5448 1739 -3777 C ATOM 2099 OD1 ASN A1055 218.172 24.338 141.453 1.00109.23 O ANISOU 2099 OD1 ASN A1055 10443 23449 7611 -5028 1731 -3992 O ATOM 2100 ND2 ASN A1055 217.145 22.519 142.276 1.00120.97 N ANISOU 2100 ND2 ASN A1055 11782 25474 8709 -6027 1731 -3664 N ATOM 2101 N GLY A1056 220.597 23.224 138.130 1.00112.25 N ANISOU 2101 N GLY A1056 12092 21716 8841 -4524 1535 -2886 N ATOM 2102 CA GLY A1056 222.018 22.997 138.301 1.00114.40 C ANISOU 2102 CA GLY A1056 12774 21361 9330 -4544 1434 -2473 C ATOM 2103 C GLY A1056 222.578 21.717 137.717 1.00110.08 C ANISOU 2103 C GLY A1056 12615 20342 8869 -4818 1353 -1950 C ATOM 2104 O GLY A1056 223.708 21.343 138.071 1.00110.03 O ANISOU 2104 O GLY A1056 12930 19919 8957 -4937 1261 -1610 O ATOM 2105 N VAL A1057 221.850 21.041 136.826 1.00110.82 N ANISOU 2105 N VAL A1057 12691 20475 8940 -4903 1370 -1886 N ATOM 2106 CA VAL A1057 222.312 19.779 136.256 1.00108.62 C ANISOU 2106 CA VAL A1057 12778 19764 8731 -5163 1272 -1413 C ATOM 2107 C VAL A1057 221.866 19.698 134.803 1.00102.28 C ANISOU 2107 C VAL A1057 11971 18722 8167 -4867 1271 -1425 C ATOM 2108 O VAL A1057 220.766 20.138 134.454 1.00107.03 O ANISOU 2108 O VAL A1057 12248 19733 8685 -4730 1366 -1769 O ATOM 2109 CB VAL A1057 221.799 18.571 137.073 1.00111.74 C ANISOU 2109 CB VAL A1057 13204 20587 8667 -5873 1275 -1225 C ATOM 2110 CG1 VAL A1057 220.278 18.514 137.058 1.00 96.46 C ANISOU 2110 CG1 VAL A1057 10878 19377 6395 -6076 1411 -1543 C ATOM 2111 CG2 VAL A1057 222.407 17.270 136.556 1.00107.17 C ANISOU 2111 CG2 VAL A1057 13057 19485 8179 -6122 1118 -726 C ATOM 2112 N ILE A1058 222.729 19.140 133.952 1.00 93.49 N ANISOU 2112 N ILE A1058 11210 16959 7351 -4758 1156 -1068 N ATOM 2113 CA ILE A1058 222.416 18.908 132.550 1.00 89.91 C ANISOU 2113 CA ILE A1058 10801 16237 7124 -4525 1142 -1020 C ATOM 2114 C ILE A1058 222.672 17.440 132.235 1.00 95.66 C ANISOU 2114 C ILE A1058 11845 16698 7804 -4899 1036 -598 C ATOM 2115 O ILE A1058 223.274 16.707 133.021 1.00 98.55 O ANISOU 2115 O ILE A1058 12440 16976 8029 -5261 942 -329 O ATOM 2116 CB ILE A1058 223.230 19.815 131.606 1.00 86.33 C ANISOU 2116 CB ILE A1058 10453 15224 7125 -3940 1091 -1047 C ATOM 2117 CG1 ILE A1058 224.727 19.558 131.785 1.00 84.96 C ANISOU 2117 CG1 ILE A1058 10631 14499 7151 -3928 970 -713 C ATOM 2118 CG2 ILE A1058 222.893 21.280 131.848 1.00 86.82 C ANISOU 2118 CG2 ILE A1058 10228 15520 7237 -3557 1153 -1476 C ATOM 2119 CD1 ILE A1058 225.602 20.349 130.840 1.00 85.48 C ANISOU 2119 CD1 ILE A1058 10818 14029 7630 -3424 916 -703 C ATOM 2120 N THR A1059 222.204 17.016 131.066 1.00 96.41 N ANISOU 2120 N THR A1059 11960 16652 8018 -4801 1031 -548 N ATOM 2121 CA THR A1059 222.352 15.639 130.619 1.00 93.44 C ANISOU 2121 CA THR A1059 11878 16009 7616 -5111 913 -181 C ATOM 2122 C THR A1059 223.549 15.503 129.684 1.00 89.18 C ANISOU 2122 C THR A1059 11646 14745 7492 -4772 784 62 C ATOM 2123 O THR A1059 224.201 16.483 129.317 1.00 88.51 O ANISOU 2123 O THR A1059 11539 14391 7701 -4323 801 -49 O ATOM 2124 CB THR A1059 221.078 15.155 129.921 1.00 95.55 C ANISOU 2124 CB THR A1059 11979 16593 7731 -5253 983 -269 C ATOM 2125 OG1 THR A1059 220.860 15.930 128.738 1.00 88.41 O ANISOU 2125 OG1 THR A1059 10936 15522 7132 -4735 1043 -467 O ATOM 2126 CG2 THR A1059 219.877 15.294 130.846 1.00104.30 C ANISOU 2126 CG2 THR A1059 12742 18488 8397 -5603 1118 -543 C ATOM 2127 N LYS A1060 223.832 14.257 129.297 1.00 82.52 N ANISOU 2127 N LYS A1060 11096 13602 6657 -5007 640 387 N ATOM 2128 CA LYS A1060 224.988 13.998 128.444 1.00 79.26 C ANISOU 2128 CA LYS A1060 10965 12543 6609 -4717 502 605 C ATOM 2129 C LYS A1060 224.776 14.551 127.041 1.00 82.54 C ANISOU 2129 C LYS A1060 11267 12779 7317 -4272 574 469 C ATOM 2130 O LYS A1060 225.690 15.151 126.461 1.00 79.33 O ANISOU 2130 O LYS A1060 10930 11984 7226 -3880 547 471 O ATOM 2131 CB LYS A1060 225.280 12.499 128.393 1.00 77.46 C ANISOU 2131 CB LYS A1060 11074 12051 6305 -5069 297 954 C ATOM 2132 CG LYS A1060 225.757 11.908 129.710 1.00 80.50 C ANISOU 2132 CG LYS A1060 11661 12473 6452 -5483 161 1145 C ATOM 2133 CD LYS A1060 226.076 10.428 129.563 1.00 82.17 C ANISOU 2133 CD LYS A1060 12250 12351 6618 -5790 -98 1487 C ATOM 2134 CE LYS A1060 227.150 10.198 128.510 1.00 82.14 C ANISOU 2134 CE LYS A1060 12459 11730 7018 -5385 -240 1610 C ATOM 2135 NZ LYS A1060 227.466 8.752 128.340 1.00 79.89 N ANISOU 2135 NZ LYS A1060 12547 11099 6706 -5640 -528 1910 N ATOM 2136 N ASP A1061 223.580 14.360 126.477 1.00 92.55 N ANISOU 2136 N ASP A1061 12360 14338 8468 -4344 660 352 N ATOM 2137 CA ASP A1061 223.305 14.872 125.138 1.00 99.32 C ANISOU 2137 CA ASP A1061 13112 15041 9586 -3939 720 222 C ATOM 2138 C ASP A1061 223.333 16.394 125.102 1.00 92.10 C ANISOU 2138 C ASP A1061 11975 14198 8821 -3520 820 -82 C ATOM 2139 O ASP A1061 223.717 16.981 124.083 1.00 93.48 O ANISOU 2139 O ASP A1061 12173 14050 9294 -3127 810 -120 O ATOM 2140 CB ASP A1061 221.957 14.348 124.638 1.00109.39 C ANISOU 2140 CB ASP A1061 14230 16658 10675 -4127 789 144 C ATOM 2141 CG ASP A1061 220.788 14.842 125.475 1.00120.05 C ANISOU 2141 CG ASP A1061 15241 18677 11697 -4309 933 -155 C ATOM 2142 OD1 ASP A1061 221.013 15.250 126.634 1.00122.70 O ANISOU 2142 OD1 ASP A1061 15514 19231 11878 -4429 955 -234 O ATOM 2143 OD2 ASP A1061 219.643 14.821 124.975 1.00126.25 O ANISOU 2143 OD2 ASP A1061 15806 19792 12371 -4329 1021 -329 O ATOM 2144 N GLU A1062 222.937 17.048 126.196 1.00 84.33 N ANISOU 2144 N GLU A1062 10785 13632 7626 -3607 900 -303 N ATOM 2145 CA GLU A1062 223.013 18.503 126.252 1.00 85.72 C ANISOU 2145 CA GLU A1062 10780 13848 7942 -3205 955 -599 C ATOM 2146 C GLU A1062 224.460 18.976 126.316 1.00 85.91 C ANISOU 2146 C GLU A1062 11022 13394 8224 -2980 870 -460 C ATOM 2147 O GLU A1062 224.810 20.004 125.725 1.00 86.85 O ANISOU 2147 O GLU A1062 11120 13288 8590 -2580 860 -588 O ATOM 2148 CB GLU A1062 222.226 19.025 127.453 1.00 87.12 C ANISOU 2148 CB GLU A1062 10669 14621 7810 -3361 1050 -894 C ATOM 2149 CG GLU A1062 220.722 18.848 127.337 1.00 92.74 C ANISOU 2149 CG GLU A1062 11083 15885 8269 -3507 1151 -1133 C ATOM 2150 CD GLU A1062 220.015 18.979 128.674 1.00 97.30 C ANISOU 2150 CD GLU A1062 11398 17115 8457 -3817 1239 -1363 C ATOM 2151 OE1 GLU A1062 220.655 18.720 129.714 1.00 96.44 O ANISOU 2151 OE1 GLU A1062 11411 17017 8214 -4084 1211 -1214 O ATOM 2152 OE2 GLU A1062 218.819 19.337 128.682 1.00 99.66 O ANISOU 2152 OE2 GLU A1062 11357 17936 8573 -3795 1332 -1705 O ATOM 2153 N ALA A1063 225.315 18.236 127.027 1.00 85.05 N ANISOU 2153 N ALA A1063 11136 13128 8053 -3246 790 -197 N ATOM 2154 CA ALA A1063 226.712 18.636 127.154 1.00 85.19 C ANISOU 2154 CA ALA A1063 11345 12729 8293 -3056 709 -73 C ATOM 2155 C ALA A1063 227.414 18.624 125.803 1.00 84.54 C ANISOU 2155 C ALA A1063 11419 12161 8540 -2754 643 54 C ATOM 2156 O ALA A1063 228.220 19.513 125.505 1.00 85.03 O ANISOU 2156 O ALA A1063 11521 11962 8823 -2449 623 10 O ATOM 2157 CB ALA A1063 227.432 17.720 128.143 1.00 83.77 C ANISOU 2157 CB ALA A1063 11378 12480 7971 -3410 612 184 C ATOM 2158 N GLU A1064 227.116 17.624 124.968 1.00 88.16 N ANISOU 2158 N GLU A1064 11966 12508 9021 -2854 605 207 N ATOM 2159 CA GLU A1064 227.723 17.562 123.642 1.00 89.84 C ANISOU 2159 CA GLU A1064 12304 12307 9526 -2585 549 310 C ATOM 2160 C GLU A1064 227.212 18.679 122.742 1.00 87.04 C ANISOU 2160 C GLU A1064 11777 11973 9320 -2236 626 79 C ATOM 2161 O GLU A1064 227.935 19.132 121.847 1.00 84.83 O ANISOU 2161 O GLU A1064 11582 11362 9289 -1965 587 114 O ATOM 2162 CB GLU A1064 227.457 16.195 123.008 1.00 91.59 C ANISOU 2162 CB GLU A1064 12656 12425 9718 -2783 480 511 C ATOM 2163 CG GLU A1064 228.206 15.952 121.706 1.00 94.95 C ANISOU 2163 CG GLU A1064 13221 12428 10428 -2540 405 630 C ATOM 2164 CD GLU A1064 227.995 14.551 121.162 1.00 99.65 C ANISOU 2164 CD GLU A1064 13963 12908 10993 -2735 308 822 C ATOM 2165 OE1 GLU A1064 227.387 13.722 121.871 1.00104.82 O ANISOU 2165 OE1 GLU A1064 14657 13770 11402 -3091 275 901 O ATOM 2166 OE2 GLU A1064 228.437 14.280 120.025 1.00100.02 O ANISOU 2166 OE2 GLU A1064 14091 12663 11249 -2546 255 891 O ATOM 2167 N LYS A1065 225.977 19.137 122.962 1.00 90.31 N ANISOU 2167 N LYS A1065 11952 12785 9575 -2245 720 -166 N ATOM 2168 CA LYS A1065 225.466 20.270 122.197 1.00 91.78 C ANISOU 2168 CA LYS A1065 11986 12987 9898 -1894 754 -412 C ATOM 2169 C LYS A1065 226.211 21.552 122.552 1.00 91.37 C ANISOU 2169 C LYS A1065 11949 12791 9975 -1635 720 -533 C ATOM 2170 O LYS A1065 226.555 22.342 121.665 1.00 91.51 O ANISOU 2170 O LYS A1065 12016 12539 10213 -1335 672 -575 O ATOM 2171 CB LYS A1065 223.964 20.426 122.433 1.00 93.46 C ANISOU 2171 CB LYS A1065 11920 13695 9894 -1956 843 -682 C ATOM 2172 CG LYS A1065 223.136 19.273 121.890 1.00 94.16 C ANISOU 2172 CG LYS A1065 11987 13925 9865 -2189 875 -582 C ATOM 2173 CD LYS A1065 221.661 19.446 122.208 1.00 97.60 C ANISOU 2173 CD LYS A1065 12115 14916 10053 -2273 971 -874 C ATOM 2174 CE LYS A1065 220.844 18.278 121.679 1.00100.07 C ANISOU 2174 CE LYS A1065 12413 15377 10230 -2539 1001 -761 C ATOM 2175 NZ LYS A1065 219.400 18.413 122.011 1.00103.25 N ANISOU 2175 NZ LYS A1065 12490 16379 10362 -2651 1101 -1061 N ATOM 2176 N LEU A1066 226.469 21.775 123.843 1.00 93.93 N ANISOU 2176 N LEU A1066 12242 13294 10154 -1768 734 -582 N ATOM 2177 CA LEU A1066 227.326 22.888 124.240 1.00 96.72 C ANISOU 2177 CA LEU A1066 12647 13474 10629 -1556 687 -657 C ATOM 2178 C LEU A1066 228.745 22.690 123.728 1.00 96.37 C ANISOU 2178 C LEU A1066 12855 12961 10800 -1496 609 -391 C ATOM 2179 O LEU A1066 229.421 23.657 123.356 1.00 96.60 O ANISOU 2179 O LEU A1066 12953 12744 11008 -1250 556 -431 O ATOM 2180 CB LEU A1066 227.330 23.036 125.761 1.00 96.69 C ANISOU 2180 CB LEU A1066 12558 13771 10408 -1744 722 -748 C ATOM 2181 CG LEU A1066 226.045 23.523 126.427 1.00 99.50 C ANISOU 2181 CG LEU A1066 12619 14647 10539 -1761 797 -1089 C ATOM 2182 CD1 LEU A1066 226.184 23.456 127.937 1.00100.13 C ANISOU 2182 CD1 LEU A1066 12639 15024 10382 -2017 834 -1126 C ATOM 2183 CD2 LEU A1066 225.719 24.938 125.978 1.00101.85 C ANISOU 2183 CD2 LEU A1066 12806 14907 10984 -1348 751 -1395 C ATOM 2184 N PHE A1067 229.213 21.440 123.706 1.00 94.02 N ANISOU 2184 N PHE A1067 12700 12547 10477 -1727 584 -130 N ATOM 2185 CA PHE A1067 230.553 21.150 123.209 1.00 91.17 C ANISOU 2185 CA PHE A1067 12549 11783 10307 -1665 501 91 C ATOM 2186 C PHE A1067 230.672 21.454 121.723 1.00 89.77 C ANISOU 2186 C PHE A1067 12405 11357 10347 -1420 480 97 C ATOM 2187 O PHE A1067 231.662 22.051 121.284 1.00 87.66 O ANISOU 2187 O PHE A1067 12233 10826 10248 -1253 431 138 O ATOM 2188 CB PHE A1067 230.906 19.691 123.494 1.00 85.21 C ANISOU 2188 CB PHE A1067 11938 10967 9471 -1945 442 333 C ATOM 2189 CG PHE A1067 232.199 19.244 122.877 1.00 81.63 C ANISOU 2189 CG PHE A1067 11673 10132 9210 -1862 340 525 C ATOM 2190 CD1 PHE A1067 233.407 19.591 123.452 1.00 80.82 C ANISOU 2190 CD1 PHE A1067 11665 9874 9170 -1821 285 580 C ATOM 2191 CD2 PHE A1067 232.205 18.446 121.743 1.00 81.18 C ANISOU 2191 CD2 PHE A1067 11684 9899 9261 -1829 296 634 C ATOM 2192 CE1 PHE A1067 234.600 19.175 122.897 1.00 77.84 C ANISOU 2192 CE1 PHE A1067 11428 9194 8952 -1740 189 721 C ATOM 2193 CE2 PHE A1067 233.397 18.023 121.183 1.00 79.05 C ANISOU 2193 CE2 PHE A1067 11556 9323 9155 -1742 196 771 C ATOM 2194 CZ PHE A1067 234.597 18.387 121.763 1.00 76.46 C ANISOU 2194 CZ PHE A1067 11304 8866 8881 -1696 143 806 C ATOM 2195 N ASN A1068 229.674 21.052 120.932 1.00 91.30 N ANISOU 2195 N ASN A1068 12518 11648 10525 -1418 516 59 N ATOM 2196 CA ASN A1068 229.712 21.329 119.500 1.00 91.06 C ANISOU 2196 CA ASN A1068 12514 11399 10684 -1203 495 63 C ATOM 2197 C ASN A1068 229.693 22.825 119.219 1.00 92.10 C ANISOU 2197 C ASN A1068 12601 11473 10918 -934 476 -123 C ATOM 2198 O ASN A1068 230.301 23.281 118.243 1.00 91.44 O ANISOU 2198 O ASN A1068 12610 11126 11006 -775 423 -73 O ATOM 2199 CB ASN A1068 228.542 20.636 118.799 1.00 94.78 C ANISOU 2199 CB ASN A1068 12895 12017 11098 -1262 539 41 C ATOM 2200 CG ASN A1068 228.647 19.124 118.848 1.00 94.89 C ANISOU 2200 CG ASN A1068 13008 12007 11040 -1519 515 253 C ATOM 2201 OD1 ASN A1068 229.733 18.570 119.020 1.00 95.17 O ANISOU 2201 OD1 ASN A1068 13203 11826 11134 -1584 440 428 O ATOM 2202 ND2 ASN A1068 227.514 18.447 118.696 1.00 95.08 N ANISOU 2202 ND2 ASN A1068 12943 12252 10930 -1666 559 228 N ATOM 2203 N GLN A1069 229.008 23.606 120.059 1.00 94.37 N ANISOU 2203 N GLN A1069 12754 12009 11093 -890 499 -346 N ATOM 2204 CA GLN A1069 229.028 25.056 119.897 1.00 95.18 C ANISOU 2204 CA GLN A1069 12847 12027 11292 -625 434 -534 C ATOM 2205 C GLN A1069 230.376 25.638 120.301 1.00 94.75 C ANISOU 2205 C GLN A1069 12944 11735 11321 -596 374 -441 C ATOM 2206 O GLN A1069 230.889 26.548 119.641 1.00 94.47 O ANISOU 2206 O GLN A1069 13010 11457 11428 -420 288 -453 O ATOM 2207 CB GLN A1069 227.913 25.699 120.717 1.00 96.41 C ANISOU 2207 CB GLN A1069 12799 12535 11299 -563 456 -838 C ATOM 2208 CG GLN A1069 226.513 25.359 120.261 1.00 96.72 C ANISOU 2208 CG GLN A1069 12655 12842 11251 -551 506 -990 C ATOM 2209 CD GLN A1069 225.473 26.204 120.963 1.00 98.12 C ANISOU 2209 CD GLN A1069 12610 13371 11301 -421 502 -1353 C ATOM 2210 OE1 GLN A1069 225.735 26.773 122.023 1.00 97.43 O ANISOU 2210 OE1 GLN A1069 12486 13393 11139 -418 490 -1471 O ATOM 2211 NE2 GLN A1069 224.287 26.299 120.372 1.00103.53 N ANISOU 2211 NE2 GLN A1069 13132 14247 11957 -302 504 -1552 N ATOM 2212 N ASP A1070 230.960 25.138 121.389 1.00 94.42 N ANISOU 2212 N ASP A1070 12928 11767 11180 -784 406 -347 N ATOM 2213 CA ASP A1070 232.256 25.643 121.816 1.00 95.13 C ANISOU 2213 CA ASP A1070 13151 11655 11340 -767 352 -261 C ATOM 2214 C ASP A1070 233.375 25.229 120.871 1.00 94.16 C ANISOU 2214 C ASP A1070 13182 11227 11368 -767 310 -41 C ATOM 2215 O ASP A1070 234.416 25.893 120.836 1.00 94.55 O ANISOU 2215 O ASP A1070 13335 11087 11502 -705 254 2 O ATOM 2216 CB ASP A1070 232.558 25.169 123.237 1.00 96.07 C ANISOU 2216 CB ASP A1070 13254 11942 11304 -974 389 -220 C ATOM 2217 CG ASP A1070 231.584 25.729 124.257 1.00100.76 C ANISOU 2217 CG ASP A1070 13676 12875 11731 -978 430 -469 C ATOM 2218 OD1 ASP A1070 230.991 26.795 123.990 1.00101.26 O ANISOU 2218 OD1 ASP A1070 13663 12976 11837 -755 396 -696 O ATOM 2219 OD2 ASP A1070 231.412 25.105 125.325 1.00104.10 O ANISOU 2219 OD2 ASP A1070 14043 13536 11973 -1205 482 -448 O ATOM 2220 N VAL A1071 233.184 24.157 120.098 1.00 90.34 N ANISOU 2220 N VAL A1071 12705 10711 10909 -839 332 83 N ATOM 2221 CA VAL A1071 234.221 23.719 119.169 1.00 85.01 C ANISOU 2221 CA VAL A1071 12145 9788 10368 -827 290 255 C ATOM 2222 C VAL A1071 234.283 24.644 117.961 1.00 89.30 C ANISOU 2222 C VAL A1071 12720 10171 11040 -649 249 208 C ATOM 2223 O VAL A1071 235.362 25.104 117.570 1.00 91.52 O ANISOU 2223 O VAL A1071 13094 10273 11405 -613 199 275 O ATOM 2224 CB VAL A1071 233.990 22.257 118.747 1.00 82.71 C ANISOU 2224 CB VAL A1071 11860 9508 10060 -953 302 387 C ATOM 2225 CG1 VAL A1071 234.791 21.938 117.499 1.00 78.96 C ANISOU 2225 CG1 VAL A1071 11456 8814 9731 -883 259 495 C ATOM 2226 CG2 VAL A1071 234.390 21.322 119.867 1.00 81.87 C ANISOU 2226 CG2 VAL A1071 11801 9459 9845 -1151 281 493 C ATOM 2227 N ASP A1072 233.129 24.933 117.349 1.00 93.89 N ANISOU 2227 N ASP A1072 13225 10823 11624 -550 261 90 N ATOM 2228 CA ASP A1072 233.139 25.778 116.158 1.00 96.02 C ANISOU 2228 CA ASP A1072 13552 10924 12009 -398 195 58 C ATOM 2229 C ASP A1072 233.577 27.200 116.484 1.00 95.97 C ANISOU 2229 C ASP A1072 13625 10810 12027 -293 104 -34 C ATOM 2230 O ASP A1072 234.144 27.885 115.624 1.00101.53 O ANISOU 2230 O ASP A1072 14442 11317 12817 -238 21 11 O ATOM 2231 CB ASP A1072 231.768 25.750 115.461 1.00106.20 C ANISOU 2231 CB ASP A1072 14745 12312 13294 -306 209 -57 C ATOM 2232 CG ASP A1072 230.667 26.492 116.230 1.00116.14 C ANISOU 2232 CG ASP A1072 15889 13772 14466 -203 199 -300 C ATOM 2233 OD1 ASP A1072 230.950 27.342 117.097 1.00118.61 O ANISOU 2233 OD1 ASP A1072 16222 14094 14751 -153 153 -400 O ATOM 2234 OD2 ASP A1072 229.482 26.217 115.946 1.00119.61 O ANISOU 2234 OD2 ASP A1072 16204 14381 14860 -164 234 -411 O ATOM 2235 N ALA A1073 233.324 27.658 117.713 1.00 89.07 N ANISOU 2235 N ALA A1073 12701 10072 11069 -280 106 -164 N ATOM 2236 CA ALA A1073 233.825 28.963 118.130 1.00 87.76 C ANISOU 2236 CA ALA A1073 12628 9791 10924 -188 4 -249 C ATOM 2237 C ALA A1073 235.347 28.988 118.118 1.00 84.15 C ANISOU 2237 C ALA A1073 12303 9161 10511 -293 -17 -70 C ATOM 2238 O ALA A1073 235.958 29.978 117.696 1.00 82.30 O ANISOU 2238 O ALA A1073 12200 8741 10331 -246 -123 -59 O ATOM 2239 CB ALA A1073 233.288 29.316 119.516 1.00 90.89 C ANISOU 2239 CB ALA A1073 12923 10402 11210 -165 22 -433 C ATOM 2240 N ALA A1074 235.978 27.905 118.575 1.00 82.69 N ANISOU 2240 N ALA A1074 12089 9038 10290 -443 66 66 N ATOM 2241 CA ALA A1074 237.427 27.796 118.458 1.00 79.14 C ANISOU 2241 CA ALA A1074 11734 8455 9881 -530 46 217 C ATOM 2242 C ALA A1074 237.844 27.664 117.001 1.00 80.02 C ANISOU 2242 C ALA A1074 11894 8431 10078 -526 19 314 C ATOM 2243 O ALA A1074 238.863 28.230 116.588 1.00 84.25 O ANISOU 2243 O ALA A1074 12519 8848 10643 -558 -37 374 O ATOM 2244 CB ALA A1074 237.935 26.607 119.273 1.00 79.10 C ANISOU 2244 CB ALA A1074 11691 8542 9822 -666 106 318 C ATOM 2245 N VAL A1075 237.065 26.928 116.206 1.00 77.43 N ANISOU 2245 N VAL A1075 11504 8142 9775 -504 59 326 N ATOM 2246 CA VAL A1075 237.382 26.773 114.789 1.00 75.10 C ANISOU 2246 CA VAL A1075 11239 7743 9551 -504 39 405 C ATOM 2247 C VAL A1075 237.285 28.114 114.072 1.00 81.12 C ANISOU 2247 C VAL A1075 12104 8373 10346 -434 -62 355 C ATOM 2248 O VAL A1075 238.109 28.430 113.206 1.00 82.95 O ANISOU 2248 O VAL A1075 12411 8505 10602 -494 -110 436 O ATOM 2249 CB VAL A1075 236.464 25.715 114.149 1.00 74.71 C ANISOU 2249 CB VAL A1075 11103 7765 9518 -493 98 418 C ATOM 2250 CG1 VAL A1075 236.678 25.660 112.645 1.00 74.61 C ANISOU 2250 CG1 VAL A1075 11116 7660 9575 -483 75 478 C ATOM 2251 CG2 VAL A1075 236.717 24.353 114.770 1.00 71.39 C ANISOU 2251 CG2 VAL A1075 10633 7428 9063 -591 151 495 C ATOM 2252 N ARG A1076 236.288 28.929 114.428 1.00 86.30 N ANISOU 2252 N ARG A1076 12768 9034 10989 -314 -117 211 N ATOM 2253 CA ARG A1076 236.144 30.234 113.788 1.00 88.36 C ANISOU 2253 CA ARG A1076 13163 9128 11282 -233 -265 155 C ATOM 2254 C ARG A1076 237.319 31.146 114.123 1.00 91.93 C ANISOU 2254 C ARG A1076 13757 9456 11715 -310 -355 206 C ATOM 2255 O ARG A1076 237.897 31.779 113.233 1.00 97.34 O ANISOU 2255 O ARG A1076 14578 9995 12412 -378 -455 283 O ATOM 2256 CB ARG A1076 234.821 30.888 114.192 1.00 91.89 C ANISOU 2256 CB ARG A1076 13576 9617 11722 -51 -333 -52 C ATOM 2257 CG ARG A1076 233.604 30.309 113.488 1.00 92.70 C ANISOU 2257 CG ARG A1076 13568 9809 11844 33 -290 -113 C ATOM 2258 CD ARG A1076 232.313 30.974 113.949 1.00 96.68 C ANISOU 2258 CD ARG A1076 14005 10401 12327 228 -364 -362 C ATOM 2259 NE ARG A1076 231.573 30.170 114.917 1.00100.92 N ANISOU 2259 NE ARG A1076 14340 11227 12778 214 -223 -462 N ATOM 2260 CZ ARG A1076 231.427 30.490 116.198 1.00104.19 C ANISOU 2260 CZ ARG A1076 14685 11788 13115 240 -213 -604 C ATOM 2261 NH1 ARG A1076 230.734 29.698 117.007 1.00104.83 N ANISOU 2261 NH1 ARG A1076 14581 12162 13089 177 -82 -681 N ATOM 2262 NH2 ARG A1076 231.968 31.605 116.672 1.00107.11 N ANISOU 2262 NH2 ARG A1076 15175 12021 13501 308 -340 -668 N ATOM 2263 N GLY A1077 237.687 31.224 115.405 1.00 88.13 N ANISOU 2263 N GLY A1077 13252 9045 11190 -327 -324 167 N ATOM 2264 CA GLY A1077 238.828 32.039 115.788 1.00 85.87 C ANISOU 2264 CA GLY A1077 13094 8656 10878 -412 -401 216 C ATOM 2265 C GLY A1077 240.118 31.604 115.122 1.00 84.96 C ANISOU 2265 C GLY A1077 13000 8526 10756 -585 -364 384 C ATOM 2266 O GLY A1077 240.982 32.436 114.830 1.00 89.07 O ANISOU 2266 O GLY A1077 13653 8942 11248 -686 -459 441 O ATOM 2267 N ILE A1078 240.268 30.303 114.872 1.00 81.09 N ANISOU 2267 N ILE A1078 12378 8154 10279 -628 -240 452 N ATOM 2268 CA ILE A1078 241.435 29.814 114.145 1.00 76.58 C ANISOU 2268 CA ILE A1078 11789 7607 9701 -762 -212 567 C ATOM 2269 C ILE A1078 241.393 30.280 112.694 1.00 79.63 C ANISOU 2269 C ILE A1078 12248 7912 10096 -809 -280 610 C ATOM 2270 O ILE A1078 242.427 30.614 112.104 1.00 84.77 O ANISOU 2270 O ILE A1078 12947 8562 10701 -956 -317 681 O ATOM 2271 CB ILE A1078 241.520 28.279 114.251 1.00 69.38 C ANISOU 2271 CB ILE A1078 10729 6821 8810 -762 -101 602 C ATOM 2272 CG1 ILE A1078 241.835 27.853 115.686 1.00 66.62 C ANISOU 2272 CG1 ILE A1078 10341 6541 8429 -769 -63 590 C ATOM 2273 CG2 ILE A1078 242.564 27.726 113.301 1.00 68.95 C ANISOU 2273 CG2 ILE A1078 10627 6814 8758 -855 -88 672 C ATOM 2274 CD1 ILE A1078 241.804 26.356 115.896 1.00 66.17 C ANISOU 2274 CD1 ILE A1078 10185 6570 8387 -772 -3 627 C ATOM 2275 N LEU A1079 240.198 30.328 112.101 1.00 76.27 N ANISOU 2275 N LEU A1079 11828 7437 9714 -702 -303 564 N ATOM 2276 CA LEU A1079 240.082 30.671 110.688 1.00 71.79 C ANISOU 2276 CA LEU A1079 11332 6793 9152 -753 -372 613 C ATOM 2277 C LEU A1079 240.227 32.171 110.450 1.00 76.13 C ANISOU 2277 C LEU A1079 12098 7166 9664 -805 -557 617 C ATOM 2278 O LEU A1079 240.838 32.584 109.458 1.00 80.49 O ANISOU 2278 O LEU A1079 12744 7674 10165 -966 -628 707 O ATOM 2279 CB LEU A1079 238.750 30.167 110.133 1.00 66.62 C ANISOU 2279 CB LEU A1079 10610 6146 8556 -618 -342 560 C ATOM 2280 CG LEU A1079 238.612 28.648 110.017 1.00 64.23 C ANISOU 2280 CG LEU A1079 10130 5990 8282 -607 -193 585 C ATOM 2281 CD1 LEU A1079 237.243 28.268 109.475 1.00 64.55 C ANISOU 2281 CD1 LEU A1079 10116 6041 8367 -490 -173 531 C ATOM 2282 CD2 LEU A1079 239.718 28.073 109.143 1.00 63.10 C ANISOU 2282 CD2 LEU A1079 9942 5910 8124 -743 -156 678 C ATOM 2283 N ARG A1080 239.679 33.001 111.336 1.00 77.84 N ANISOU 2283 N ARG A1080 12402 7284 9890 -682 -652 515 N ATOM 2284 CA ARG A1080 239.814 34.444 111.171 1.00 81.37 C ANISOU 2284 CA ARG A1080 13088 7523 10305 -719 -872 511 C ATOM 2285 C ARG A1080 241.157 34.967 111.663 1.00 89.84 C ANISOU 2285 C ARG A1080 14251 8586 11298 -906 -905 589 C ATOM 2286 O ARG A1080 241.382 36.181 111.625 1.00 94.16 O ANISOU 2286 O ARG A1080 15023 8951 11803 -969 -1104 599 O ATOM 2287 CB ARG A1080 238.680 35.178 111.891 1.00 80.25 C ANISOU 2287 CB ARG A1080 13004 7278 10209 -485 -996 333 C ATOM 2288 CG ARG A1080 238.568 34.891 113.377 1.00 78.47 C ANISOU 2288 CG ARG A1080 12648 7186 9983 -383 -891 222 C ATOM 2289 CD ARG A1080 237.278 35.472 113.931 1.00 78.80 C ANISOU 2289 CD ARG A1080 12686 7196 10059 -134 -996 2 C ATOM 2290 NE ARG A1080 237.222 36.923 113.771 1.00 79.46 N ANISOU 2290 NE ARG A1080 13020 7025 10147 -74 -1274 -63 N ATOM 2291 CZ ARG A1080 236.133 37.656 113.977 1.00 82.37 C ANISOU 2291 CZ ARG A1080 13432 7312 10554 168 -1446 -276 C ATOM 2292 NH1 ARG A1080 235.001 37.076 114.350 1.00 80.90 N ANISOU 2292 NH1 ARG A1080 13027 7321 10390 354 -1341 -451 N ATOM 2293 NH2 ARG A1080 236.174 38.971 113.807 1.00 85.45 N ANISOU 2293 NH2 ARG A1080 14086 7430 10950 218 -1742 -327 N ATOM 2294 N ASN A1081 242.044 34.088 112.117 1.00 91.42 N ANISOU 2294 N ASN A1081 14293 8969 11473 -994 -736 638 N ATOM 2295 CA ASN A1081 243.389 34.455 112.537 1.00 93.52 C ANISOU 2295 CA ASN A1081 14607 9272 11655 -1179 -747 706 C ATOM 2296 C ASN A1081 244.382 34.086 111.443 1.00 95.69 C ANISOU 2296 C ASN A1081 14835 9667 11855 -1403 -703 818 C ATOM 2297 O ASN A1081 244.363 32.958 110.937 1.00 98.98 O ANISOU 2297 O ASN A1081 15073 10231 12304 -1380 -570 825 O ATOM 2298 CB ASN A1081 243.761 33.751 113.842 1.00 94.23 C ANISOU 2298 CB ASN A1081 14547 9500 11757 -1118 -610 663 C ATOM 2299 CG ASN A1081 244.947 34.388 114.531 1.00 95.46 C ANISOU 2299 CG ASN A1081 14778 9659 11833 -1263 -653 698 C ATOM 2300 OD1 ASN A1081 246.041 34.450 113.973 1.00 96.66 O ANISOU 2300 OD1 ASN A1081 14935 9886 11904 -1467 -654 782 O ATOM 2301 ND2 ASN A1081 244.739 34.858 115.754 1.00 97.31 N ANISOU 2301 ND2 ASN A1081 15055 9840 12076 -1167 -685 620 N ATOM 2302 N ALA A1082 245.249 35.033 111.082 1.00 93.98 N ANISOU 2302 N ALA A1082 14778 9404 11528 -1631 -824 895 N ATOM 2303 CA ALA A1082 246.256 34.774 110.063 1.00 92.61 C ANISOU 2303 CA ALA A1082 14542 9401 11245 -1883 -785 981 C ATOM 2304 C ALA A1082 247.498 34.090 110.617 1.00 90.87 C ANISOU 2304 C ALA A1082 14131 9422 10971 -1967 -649 969 C ATOM 2305 O ALA A1082 248.310 33.587 109.832 1.00 89.95 O ANISOU 2305 O ALA A1082 13882 9522 10775 -2126 -583 990 O ATOM 2306 CB ALA A1082 246.652 36.077 109.368 1.00 94.38 C ANISOU 2306 CB ALA A1082 15024 9499 11335 -2146 -987 1077 C ATOM 2307 N LYS A1083 247.667 34.064 111.937 1.00 89.34 N ANISOU 2307 N LYS A1083 13916 9213 10816 -1860 -617 920 N ATOM 2308 CA LYS A1083 248.772 33.360 112.573 1.00 85.67 C ANISOU 2308 CA LYS A1083 13274 8959 10318 -1899 -506 895 C ATOM 2309 C LYS A1083 248.419 31.918 112.920 1.00 80.69 C ANISOU 2309 C LYS A1083 12435 8425 9798 -1692 -370 833 C ATOM 2310 O LYS A1083 249.315 31.137 113.262 1.00 80.75 O ANISOU 2310 O LYS A1083 12284 8608 9790 -1701 -298 801 O ATOM 2311 CB LYS A1083 249.211 34.116 113.837 1.00 82.52 C ANISOU 2311 CB LYS A1083 12979 8488 9888 -1917 -559 886 C ATOM 2312 CG LYS A1083 250.572 33.723 114.397 1.00 80.02 C ANISOU 2312 CG LYS A1083 12522 8384 9498 -2022 -488 872 C ATOM 2313 CD LYS A1083 251.452 34.947 114.617 1.00 79.62 C ANISOU 2313 CD LYS A1083 12629 8314 9310 -2257 -595 921 C ATOM 2314 CE LYS A1083 250.720 36.028 115.398 1.00 80.92 C ANISOU 2314 CE LYS A1083 13030 8203 9512 -2177 -722 922 C ATOM 2315 NZ LYS A1083 251.541 37.262 115.542 1.00 83.34 N ANISOU 2315 NZ LYS A1083 13529 8456 9681 -2422 -858 981 N ATOM 2316 N LEU A1084 247.142 31.547 112.822 1.00 76.00 N ANISOU 2316 N LEU A1084 11846 7723 9308 -1512 -352 811 N ATOM 2317 CA LEU A1084 246.680 30.205 113.148 1.00 74.51 C ANISOU 2317 CA LEU A1084 11497 7601 9210 -1344 -247 769 C ATOM 2318 C LEU A1084 246.133 29.437 111.957 1.00 74.40 C ANISOU 2318 C LEU A1084 11400 7628 9242 -1304 -208 773 C ATOM 2319 O LEU A1084 246.198 28.206 111.954 1.00 76.96 O ANISOU 2319 O LEU A1084 11578 8048 9614 -1224 -138 746 O ATOM 2320 CB LEU A1084 245.595 30.267 114.230 1.00 73.12 C ANISOU 2320 CB LEU A1084 11369 7314 9099 -1180 -243 725 C ATOM 2321 CG LEU A1084 245.989 30.868 115.580 1.00 74.44 C ANISOU 2321 CG LEU A1084 11598 7453 9232 -1186 -270 702 C ATOM 2322 CD1 LEU A1084 244.756 31.144 116.423 1.00 76.55 C ANISOU 2322 CD1 LEU A1084 11911 7636 9540 -1037 -281 631 C ATOM 2323 CD2 LEU A1084 246.928 29.930 116.314 1.00 74.94 C ANISOU 2323 CD2 LEU A1084 11537 7652 9285 -1203 -205 705 C ATOM 2324 N LYS A1085 245.594 30.128 110.944 1.00 75.25 N ANISOU 2324 N LYS A1085 11609 7649 9333 -1357 -269 805 N ATOM 2325 CA LYS A1085 244.999 29.413 109.813 1.00 76.80 C ANISOU 2325 CA LYS A1085 11726 7881 9573 -1316 -229 807 C ATOM 2326 C LYS A1085 246.032 28.668 108.977 1.00 80.74 C ANISOU 2326 C LYS A1085 12067 8589 10021 -1424 -178 801 C ATOM 2327 O LYS A1085 245.790 27.491 108.648 1.00 80.91 O ANISOU 2327 O LYS A1085 11950 8685 10108 -1319 -112 764 O ATOM 2328 CB LYS A1085 244.173 30.375 108.955 1.00 76.24 C ANISOU 2328 CB LYS A1085 11817 7658 9493 -1347 -329 842 C ATOM 2329 CG LYS A1085 243.565 29.705 107.730 1.00 74.72 C ANISOU 2329 CG LYS A1085 11548 7504 9337 -1318 -291 849 C ATOM 2330 CD LYS A1085 242.915 30.705 106.791 1.00 74.01 C ANISOU 2330 CD LYS A1085 11633 7265 9221 -1379 -417 893 C ATOM 2331 CE LYS A1085 242.418 30.015 105.529 1.00 74.58 C ANISOU 2331 CE LYS A1085 11620 7398 9319 -1372 -372 905 C ATOM 2332 NZ LYS A1085 241.814 30.973 104.564 1.00 74.83 N ANISOU 2332 NZ LYS A1085 11835 7278 9319 -1444 -514 956 N ATOM 2333 N PRO A1086 247.169 29.262 108.577 1.00 82.06 N ANISOU 2333 N PRO A1086 12238 8876 10063 -1636 -211 820 N ATOM 2334 CA PRO A1086 248.138 28.486 107.782 1.00 82.03 C ANISOU 2334 CA PRO A1086 12037 9133 9999 -1723 -158 768 C ATOM 2335 C PRO A1086 248.603 27.222 108.478 1.00 78.92 C ANISOU 2335 C PRO A1086 11463 8847 9675 -1563 -99 678 C ATOM 2336 O PRO A1086 248.824 26.197 107.820 1.00 81.29 O ANISOU 2336 O PRO A1086 11596 9292 9998 -1505 -65 605 O ATOM 2337 CB PRO A1086 249.290 29.477 107.570 1.00 83.56 C ANISOU 2337 CB PRO A1086 12272 9456 10019 -1999 -208 795 C ATOM 2338 CG PRO A1086 248.666 30.812 107.700 1.00 83.70 C ANISOU 2338 CG PRO A1086 12559 9230 10014 -2080 -318 895 C ATOM 2339 CD PRO A1086 247.613 30.658 108.749 1.00 84.29 C ANISOU 2339 CD PRO A1086 12702 9085 10239 -1821 -312 879 C ATOM 2340 N VAL A1087 248.755 27.266 109.803 1.00 76.86 N ANISOU 2340 N VAL A1087 11245 8512 9447 -1487 -107 676 N ATOM 2341 CA VAL A1087 249.090 26.059 110.548 1.00 78.10 C ANISOU 2341 CA VAL A1087 11276 8724 9675 -1332 -88 606 C ATOM 2342 C VAL A1087 247.927 25.079 110.518 1.00 80.87 C ANISOU 2342 C VAL A1087 11623 8957 10146 -1156 -68 612 C ATOM 2343 O VAL A1087 248.119 23.871 110.335 1.00 84.19 O ANISOU 2343 O VAL A1087 11924 9446 10619 -1052 -74 549 O ATOM 2344 CB VAL A1087 249.490 26.418 111.989 1.00 74.27 C ANISOU 2344 CB VAL A1087 10857 8181 9180 -1322 -108 617 C ATOM 2345 CG1 VAL A1087 249.825 25.161 112.772 1.00 73.75 C ANISOU 2345 CG1 VAL A1087 10692 8149 9181 -1174 -122 558 C ATOM 2346 CG2 VAL A1087 250.662 27.385 111.987 1.00 79.73 C ANISOU 2346 CG2 VAL A1087 11553 9000 9740 -1516 -131 613 C ATOM 2347 N TYR A1088 246.701 25.584 110.680 1.00 81.99 N ANISOU 2347 N TYR A1088 11896 8929 10327 -1119 -59 674 N ATOM 2348 CA TYR A1088 245.534 24.708 110.719 1.00 84.90 C ANISOU 2348 CA TYR A1088 12260 9212 10787 -980 -34 680 C ATOM 2349 C TYR A1088 245.303 24.024 109.376 1.00 87.09 C ANISOU 2349 C TYR A1088 12448 9550 11093 -961 -18 659 C ATOM 2350 O TYR A1088 244.891 22.859 109.330 1.00 88.10 O ANISOU 2350 O TYR A1088 12517 9669 11288 -855 -14 639 O ATOM 2351 CB TYR A1088 244.302 25.510 111.134 1.00 84.93 C ANISOU 2351 CB TYR A1088 12393 9069 10806 -947 -31 714 C ATOM 2352 CG TYR A1088 243.044 24.684 111.297 1.00 85.80 C ANISOU 2352 CG TYR A1088 12488 9131 10981 -833 2 711 C ATOM 2353 CD1 TYR A1088 242.815 23.954 112.456 1.00 85.23 C ANISOU 2353 CD1 TYR A1088 12407 9057 10920 -784 10 710 C ATOM 2354 CD2 TYR A1088 242.080 24.643 110.297 1.00 87.78 C ANISOU 2354 CD2 TYR A1088 12737 9349 11264 -797 18 715 C ATOM 2355 CE1 TYR A1088 241.664 23.201 112.612 1.00 84.14 C ANISOU 2355 CE1 TYR A1088 12258 8903 10810 -728 36 714 C ATOM 2356 CE2 TYR A1088 240.926 23.892 110.445 1.00 86.13 C ANISOU 2356 CE2 TYR A1088 12506 9123 11097 -714 51 708 C ATOM 2357 CZ TYR A1088 240.725 23.173 111.605 1.00 84.56 C ANISOU 2357 CZ TYR A1088 12296 8939 10893 -691 61 709 C ATOM 2358 OH TYR A1088 239.582 22.424 111.761 1.00 83.23 O ANISOU 2358 OH TYR A1088 12108 8779 10735 -655 90 709 O ATOM 2359 N ASP A1089 245.570 24.727 108.272 1.00 88.36 N ANISOU 2359 N ASP A1089 12608 9773 11193 -1080 -20 668 N ATOM 2360 CA ASP A1089 245.324 24.150 106.953 1.00 88.03 C ANISOU 2360 CA ASP A1089 12477 9804 11165 -1076 0 645 C ATOM 2361 C ASP A1089 246.315 23.038 106.636 1.00 88.11 C ANISOU 2361 C ASP A1089 12304 9997 11176 -1038 -4 543 C ATOM 2362 O ASP A1089 245.938 22.008 106.063 1.00 92.81 O ANISOU 2362 O ASP A1089 12820 10609 11836 -936 -1 501 O ATOM 2363 CB ASP A1089 245.386 25.240 105.884 1.00 91.45 C ANISOU 2363 CB ASP A1089 12973 10266 11509 -1248 -18 689 C ATOM 2364 CG ASP A1089 244.256 26.238 106.005 1.00 96.99 C ANISOU 2364 CG ASP A1089 13862 10758 12230 -1239 -56 762 C ATOM 2365 OD1 ASP A1089 243.258 25.924 106.685 1.00100.11 O ANISOU 2365 OD1 ASP A1089 14292 11032 12712 -1085 -40 759 O ATOM 2366 OD2 ASP A1089 244.365 27.337 105.422 1.00100.45 O ANISOU 2366 OD2 ASP A1089 14417 11163 12587 -1392 -119 814 O ATOM 2367 N SER A1090 247.584 23.223 106.998 1.00 81.88 N ANISOU 2367 N SER A1090 11443 9354 10315 -1108 -25 486 N ATOM 2368 CA SER A1090 248.606 22.235 106.677 1.00 78.91 C ANISOU 2368 CA SER A1090 10870 9182 9930 -1051 -52 345 C ATOM 2369 C SER A1090 248.514 20.979 107.533 1.00 79.59 C ANISOU 2369 C SER A1090 10940 9173 10128 -847 -114 299 C ATOM 2370 O SER A1090 249.178 19.987 107.213 1.00 83.47 O ANISOU 2370 O SER A1090 11283 9791 10642 -745 -174 163 O ATOM 2371 CB SER A1090 249.994 22.859 106.823 1.00 81.32 C ANISOU 2371 CB SER A1090 11089 9703 10107 -1195 -62 280 C ATOM 2372 OG SER A1090 250.251 23.220 108.167 1.00 80.66 O ANISOU 2372 OG SER A1090 11100 9517 10032 -1179 -85 322 O ATOM 2373 N LEU A1091 247.719 20.990 108.601 1.00 80.42 N ANISOU 2373 N LEU A1091 11194 9069 10291 -793 -118 397 N ATOM 2374 CA LEU A1091 247.582 19.835 109.476 1.00 81.92 C ANISOU 2374 CA LEU A1091 11409 9154 10561 -650 -197 383 C ATOM 2375 C LEU A1091 246.511 18.881 108.962 1.00 80.05 C ANISOU 2375 C LEU A1091 11195 8814 10405 -560 -210 405 C ATOM 2376 O LEU A1091 245.558 19.287 108.290 1.00 81.82 O ANISOU 2376 O LEU A1091 11457 8999 10633 -601 -135 465 O ATOM 2377 CB LEU A1091 247.235 20.269 110.902 1.00 75.37 C ANISOU 2377 CB LEU A1091 10721 8189 9727 -673 -194 476 C ATOM 2378 CG LEU A1091 248.305 21.005 111.706 1.00 74.43 C ANISOU 2378 CG LEU A1091 10598 8141 9540 -741 -205 457 C ATOM 2379 CD1 LEU A1091 247.783 21.344 113.094 1.00 71.71 C ANISOU 2379 CD1 LEU A1091 10392 7660 9193 -756 -200 545 C ATOM 2380 CD2 LEU A1091 249.568 20.171 111.797 1.00 78.49 C ANISOU 2380 CD2 LEU A1091 10985 8780 10058 -662 -304 330 C ATOM 2381 N ASP A1092 246.675 17.600 109.289 1.00 79.36 N ANISOU 2381 N ASP A1092 11101 8674 10380 -438 -326 355 N ATOM 2382 CA ASP A1092 245.664 16.607 108.965 1.00 83.02 C ANISOU 2382 CA ASP A1092 11616 9018 10910 -370 -364 389 C ATOM 2383 C ASP A1092 244.507 16.704 109.957 1.00 83.49 C ANISOU 2383 C ASP A1092 11835 8924 10965 -427 -332 529 C ATOM 2384 O ASP A1092 244.487 17.558 110.847 1.00 85.56 O ANISOU 2384 O ASP A1092 12156 9176 11178 -499 -280 584 O ATOM 2385 CB ASP A1092 246.273 15.204 108.942 1.00 88.79 C ANISOU 2385 CB ASP A1092 12309 9725 11702 -226 -542 281 C ATOM 2386 CG ASP A1092 246.964 14.828 110.248 1.00 93.72 C ANISOU 2386 CG ASP A1092 13007 10278 12326 -188 -675 276 C ATOM 2387 OD1 ASP A1092 246.673 15.441 111.296 1.00 95.61 O ANISOU 2387 OD1 ASP A1092 13352 10454 12523 -284 -623 388 O ATOM 2388 OD2 ASP A1092 247.799 13.898 110.226 1.00 95.99 O ANISOU 2388 OD2 ASP A1092 13245 10573 12656 -52 -849 147 O ATOM 2389 N ALA A1093 243.534 15.802 109.813 1.00 84.22 N ANISOU 2389 N ALA A1093 11988 8917 11094 -402 -369 574 N ATOM 2390 CA ALA A1093 242.339 15.868 110.648 1.00 80.81 C ANISOU 2390 CA ALA A1093 11675 8401 10627 -484 -326 688 C ATOM 2391 C ALA A1093 242.669 15.656 112.121 1.00 79.94 C ANISOU 2391 C ALA A1093 11663 8235 10476 -528 -407 733 C ATOM 2392 O ALA A1093 242.090 16.313 112.995 1.00 80.82 O ANISOU 2392 O ALA A1093 11830 8354 10525 -617 -332 794 O ATOM 2393 CB ALA A1093 241.312 14.840 110.175 1.00 79.74 C ANISOU 2393 CB ALA A1093 11582 8196 10520 -477 -363 724 C ATOM 2394 N VAL A1094 243.604 14.752 112.417 1.00 77.55 N ANISOU 2394 N VAL A1094 11380 7882 10205 -460 -573 689 N ATOM 2395 CA VAL A1094 243.915 14.436 113.808 1.00 73.92 C ANISOU 2395 CA VAL A1094 11035 7349 9703 -510 -681 743 C ATOM 2396 C VAL A1094 244.689 15.576 114.459 1.00 70.26 C ANISOU 2396 C VAL A1094 10529 6970 9198 -538 -605 722 C ATOM 2397 O VAL A1094 244.368 16.010 115.571 1.00 71.02 O ANISOU 2397 O VAL A1094 10702 7055 9227 -638 -569 794 O ATOM 2398 CB VAL A1094 244.687 13.108 113.897 1.00 78.53 C ANISOU 2398 CB VAL A1094 11673 7825 10340 -407 -926 690 C ATOM 2399 CG1 VAL A1094 245.076 12.817 115.338 1.00 79.75 C ANISOU 2399 CG1 VAL A1094 11964 7892 10445 -469 -1061 753 C ATOM 2400 CG2 VAL A1094 243.853 11.974 113.328 1.00 78.81 C ANISOU 2400 CG2 VAL A1094 11785 7749 10409 -398 -1024 724 C ATOM 2401 N ARG A1095 245.723 16.077 113.780 1.00 71.22 N ANISOU 2401 N ARG A1095 10522 7196 9345 -467 -582 616 N ATOM 2402 CA ARG A1095 246.509 17.167 114.343 1.00 72.72 C ANISOU 2402 CA ARG A1095 10677 7469 9484 -513 -519 598 C ATOM 2403 C ARG A1095 245.720 18.466 114.436 1.00 73.03 C ANISOU 2403 C ARG A1095 10742 7533 9474 -614 -354 663 C ATOM 2404 O ARG A1095 246.050 19.317 115.268 1.00 76.20 O ANISOU 2404 O ARG A1095 11173 7956 9825 -672 -318 680 O ATOM 2405 CB ARG A1095 247.782 17.387 113.523 1.00 78.69 C ANISOU 2405 CB ARG A1095 11278 8372 10250 -451 -534 463 C ATOM 2406 CG ARG A1095 248.785 16.247 113.626 1.00 80.88 C ANISOU 2406 CG ARG A1095 11508 8651 10570 -316 -726 348 C ATOM 2407 CD ARG A1095 250.101 16.618 112.968 1.00 83.66 C ANISOU 2407 CD ARG A1095 11670 9220 10897 -275 -724 184 C ATOM 2408 NE ARG A1095 251.127 15.600 113.169 1.00 86.01 N ANISOU 2408 NE ARG A1095 11904 9541 11234 -115 -927 33 N ATOM 2409 CZ ARG A1095 251.387 14.620 112.310 1.00 91.10 C ANISOU 2409 CZ ARG A1095 12452 10225 11938 37 -1050 -115 C ATOM 2410 NH1 ARG A1095 250.694 14.521 111.183 1.00 93.63 N ANISOU 2410 NH1 ARG A1095 12725 10570 12278 30 -969 -114 N ATOM 2411 NH2 ARG A1095 252.341 13.737 112.576 1.00 94.12 N ANISOU 2411 NH2 ARG A1095 12783 10619 12360 209 -1268 -279 N ATOM 2412 N ARG A1096 244.691 18.642 113.605 1.00 71.09 N ANISOU 2412 N ARG A1096 10488 7280 9243 -622 -270 686 N ATOM 2413 CA ARG A1096 243.824 19.805 113.760 1.00 72.23 C ANISOU 2413 CA ARG A1096 10671 7426 9346 -686 -154 725 C ATOM 2414 C ARG A1096 243.078 19.754 115.087 1.00 68.91 C ANISOU 2414 C ARG A1096 10338 6970 8876 -740 -149 780 C ATOM 2415 O ARG A1096 242.891 20.786 115.742 1.00 69.12 O ANISOU 2415 O ARG A1096 10393 7017 8854 -780 -93 777 O ATOM 2416 CB ARG A1096 242.844 19.893 112.590 1.00 74.04 C ANISOU 2416 CB ARG A1096 10873 7653 9605 -667 -91 727 C ATOM 2417 CG ARG A1096 243.460 20.414 111.302 1.00 77.19 C ANISOU 2417 CG ARG A1096 11195 8117 10017 -664 -68 680 C ATOM 2418 CD ARG A1096 242.417 20.540 110.204 1.00 77.47 C ANISOU 2418 CD ARG A1096 11221 8137 10076 -652 -13 692 C ATOM 2419 NE ARG A1096 243.014 20.878 108.914 1.00 80.21 N ANISOU 2419 NE ARG A1096 11495 8562 10419 -678 -3 654 N ATOM 2420 CZ ARG A1096 242.329 21.340 107.874 1.00 81.19 C ANISOU 2420 CZ ARG A1096 11623 8679 10546 -697 36 668 C ATOM 2421 NH1 ARG A1096 241.019 21.525 107.971 1.00 87.41 N ANISOU 2421 NH1 ARG A1096 12472 9386 11353 -665 67 701 N ATOM 2422 NH2 ARG A1096 242.951 21.620 106.736 1.00 77.02 N ANISOU 2422 NH2 ARG A1096 11030 8246 9988 -757 39 640 N ATOM 2423 N ALA A1097 242.652 18.558 115.502 1.00 64.35 N ANISOU 2423 N ALA A1097 9808 6347 8294 -756 -221 823 N ATOM 2424 CA ALA A1097 241.983 18.416 116.792 1.00 62.98 C ANISOU 2424 CA ALA A1097 9712 6179 8038 -855 -223 878 C ATOM 2425 C ALA A1097 242.919 18.772 117.939 1.00 63.36 C ANISOU 2425 C ALA A1097 9797 6232 8046 -889 -266 881 C ATOM 2426 O ALA A1097 242.501 19.400 118.919 1.00 63.80 O ANISOU 2426 O ALA A1097 9879 6339 8024 -963 -211 890 O ATOM 2427 CB ALA A1097 241.453 16.993 116.954 1.00 62.68 C ANISOU 2427 CB ALA A1097 9747 6085 7985 -909 -325 943 C ATOM 2428 N ALA A1098 244.192 18.382 117.834 1.00 64.64 N ANISOU 2428 N ALA A1098 9947 6358 8254 -828 -367 856 N ATOM 2429 CA ALA A1098 245.164 18.759 118.854 1.00 66.84 C ANISOU 2429 CA ALA A1098 10250 6649 8497 -852 -409 850 C ATOM 2430 C ALA A1098 245.315 20.273 118.936 1.00 68.35 C ANISOU 2430 C ALA A1098 10402 6909 8660 -871 -288 815 C ATOM 2431 O ALA A1098 245.470 20.832 120.029 1.00 70.45 O ANISOU 2431 O ALA A1098 10708 7195 8865 -930 -274 827 O ATOM 2432 CB ALA A1098 246.512 18.097 118.567 1.00 68.07 C ANISOU 2432 CB ALA A1098 10369 6784 8710 -757 -546 792 C ATOM 2433 N LEU A1099 245.266 20.954 117.789 1.00 65.21 N ANISOU 2433 N LEU A1099 9940 6540 8298 -832 -216 773 N ATOM 2434 CA LEU A1099 245.320 22.413 117.788 1.00 63.06 C ANISOU 2434 CA LEU A1099 9670 6295 7993 -862 -139 749 C ATOM 2435 C LEU A1099 244.065 23.003 118.419 1.00 62.85 C ANISOU 2435 C LEU A1099 9692 6263 7923 -887 -76 753 C ATOM 2436 O LEU A1099 244.144 23.919 119.246 1.00 63.39 O ANISOU 2436 O LEU A1099 9798 6345 7944 -917 -58 732 O ATOM 2437 CB LEU A1099 245.503 22.927 116.362 1.00 62.83 C ANISOU 2437 CB LEU A1099 9589 6288 7997 -844 -108 718 C ATOM 2438 CG LEU A1099 245.621 24.440 116.187 1.00 62.76 C ANISOU 2438 CG LEU A1099 9621 6275 7949 -897 -74 706 C ATOM 2439 CD1 LEU A1099 246.755 24.994 117.032 1.00 63.61 C ANISOU 2439 CD1 LEU A1099 9747 6416 8005 -955 -102 698 C ATOM 2440 CD2 LEU A1099 245.830 24.779 114.722 1.00 63.01 C ANISOU 2440 CD2 LEU A1099 9615 6334 7990 -920 -66 695 C ATOM 2441 N ILE A1100 242.895 22.486 118.037 1.00 64.26 N ANISOU 2441 N ILE A1100 9861 6443 8112 -871 -46 761 N ATOM 2442 CA ILE A1100 241.649 22.904 118.673 1.00 64.99 C ANISOU 2442 CA ILE A1100 9963 6585 8146 -891 10 731 C ATOM 2443 C ILE A1100 241.690 22.602 120.166 1.00 67.47 C ANISOU 2443 C ILE A1100 10309 6954 8373 -978 -8 751 C ATOM 2444 O ILE A1100 241.190 23.381 120.988 1.00 69.66 O ANISOU 2444 O ILE A1100 10584 7301 8582 -999 33 693 O ATOM 2445 CB ILE A1100 240.449 22.224 117.985 1.00 63.80 C ANISOU 2445 CB ILE A1100 9778 6457 8006 -877 41 734 C ATOM 2446 CG1 ILE A1100 240.373 22.640 116.516 1.00 62.63 C ANISOU 2446 CG1 ILE A1100 9602 6258 7936 -797 58 712 C ATOM 2447 CG2 ILE A1100 239.153 22.569 118.694 1.00 66.35 C ANISOU 2447 CG2 ILE A1100 10076 6891 8245 -905 99 673 C ATOM 2448 CD1 ILE A1100 239.307 21.913 115.730 1.00 62.27 C ANISOU 2448 CD1 ILE A1100 9520 6230 7912 -778 84 718 C ATOM 2449 N ASN A1101 242.297 21.472 120.539 1.00 65.85 N ANISOU 2449 N ASN A1101 10139 6717 8164 -1029 -87 824 N ATOM 2450 CA ASN A1101 242.439 21.133 121.950 1.00 66.43 C ANISOU 2450 CA ASN A1101 10266 6830 8145 -1137 -129 863 C ATOM 2451 C ASN A1101 243.189 22.227 122.701 1.00 71.10 C ANISOU 2451 C ASN A1101 10862 7440 8712 -1132 -111 821 C ATOM 2452 O ASN A1101 242.809 22.596 123.819 1.00 71.41 O ANISOU 2452 O ASN A1101 10913 7564 8656 -1208 -82 801 O ATOM 2453 CB ASN A1101 243.151 19.785 122.086 1.00 64.86 C ANISOU 2453 CB ASN A1101 10135 6545 7966 -1167 -269 944 C ATOM 2454 CG ASN A1101 243.117 19.234 123.502 1.00 65.53 C ANISOU 2454 CG ASN A1101 10306 6654 7937 -1315 -342 1012 C ATOM 2455 OD1 ASN A1101 243.231 19.970 124.480 1.00 66.13 O ANISOU 2455 OD1 ASN A1101 10381 6805 7940 -1371 -298 989 O ATOM 2456 ND2 ASN A1101 242.957 17.921 123.613 1.00 66.83 N ANISOU 2456 ND2 ASN A1101 10563 6751 8079 -1392 -472 1097 N ATOM 2457 N MET A1102 244.247 22.771 122.096 1.00 75.20 N ANISOU 2457 N MET A1102 11368 7902 9302 -1059 -127 800 N ATOM 2458 CA MET A1102 244.997 23.839 122.749 1.00 75.59 C ANISOU 2458 CA MET A1102 11434 7964 9324 -1070 -118 766 C ATOM 2459 C MET A1102 244.212 25.144 122.753 1.00 74.09 C ANISOU 2459 C MET A1102 11242 7797 9110 -1043 -48 689 C ATOM 2460 O MET A1102 244.242 25.890 123.739 1.00 71.05 O ANISOU 2460 O MET A1102 10881 7449 8666 -1070 -39 647 O ATOM 2461 CB MET A1102 246.347 24.027 122.062 1.00 74.98 C ANISOU 2461 CB MET A1102 11334 7853 9302 -1034 -159 762 C ATOM 2462 CG MET A1102 247.236 22.803 122.117 1.00 75.02 C ANISOU 2462 CG MET A1102 11326 7843 9334 -1020 -260 792 C ATOM 2463 SD MET A1102 248.830 23.096 121.336 1.00 76.98 S ANISOU 2463 SD MET A1102 11496 8136 9618 -980 -299 735 S ATOM 2464 CE MET A1102 249.505 24.354 122.419 1.00 79.16 C ANISOU 2464 CE MET A1102 11812 8445 9820 -1057 -274 726 C ATOM 2465 N VAL A1103 243.507 25.438 121.657 1.00 74.87 N ANISOU 2465 N VAL A1103 11320 7869 9257 -978 -19 657 N ATOM 2466 CA VAL A1103 242.717 26.663 121.589 1.00 76.89 C ANISOU 2466 CA VAL A1103 11591 8123 9502 -921 4 564 C ATOM 2467 C VAL A1103 241.577 26.626 122.597 1.00 78.15 C ANISOU 2467 C VAL A1103 11710 8403 9579 -932 44 489 C ATOM 2468 O VAL A1103 241.184 27.665 123.142 1.00 80.03 O ANISOU 2468 O VAL A1103 11955 8673 9781 -887 41 380 O ATOM 2469 CB VAL A1103 242.201 26.879 120.154 1.00 75.64 C ANISOU 2469 CB VAL A1103 11426 7903 9412 -852 5 551 C ATOM 2470 CG1 VAL A1103 241.265 28.077 120.089 1.00 77.02 C ANISOU 2470 CG1 VAL A1103 11630 8055 9580 -767 -12 438 C ATOM 2471 CG2 VAL A1103 243.368 27.061 119.197 1.00 74.10 C ANISOU 2471 CG2 VAL A1103 11257 7636 9262 -877 -32 608 C ATOM 2472 N PHE A1104 241.040 25.437 122.877 1.00 77.46 N ANISOU 2472 N PHE A1104 11582 8401 9448 -1003 70 536 N ATOM 2473 CA PHE A1104 239.941 25.328 123.831 1.00 80.96 C ANISOU 2473 CA PHE A1104 11968 9019 9775 -1061 116 462 C ATOM 2474 C PHE A1104 240.385 25.702 125.241 1.00 81.04 C ANISOU 2474 C PHE A1104 11994 9105 9694 -1136 109 437 C ATOM 2475 O PHE A1104 239.632 26.342 125.984 1.00 83.34 O ANISOU 2475 O PHE A1104 12226 9543 9897 -1130 145 304 O ATOM 2476 CB PHE A1104 239.369 23.911 123.800 1.00 78.57 C ANISOU 2476 CB PHE A1104 11645 8785 9422 -1174 124 547 C ATOM 2477 CG PHE A1104 237.921 23.834 124.184 1.00 80.04 C ANISOU 2477 CG PHE A1104 11738 9184 9490 -1228 189 449 C ATOM 2478 CD1 PHE A1104 237.524 24.055 125.492 1.00 82.84 C ANISOU 2478 CD1 PHE A1104 12044 9736 9694 -1333 219 374 C ATOM 2479 CD2 PHE A1104 236.955 23.558 123.233 1.00 79.86 C ANISOU 2479 CD2 PHE A1104 11658 9193 9494 -1180 222 417 C ATOM 2480 CE1 PHE A1104 236.192 23.989 125.846 1.00 86.09 C ANISOU 2480 CE1 PHE A1104 12336 10404 9972 -1397 284 254 C ATOM 2481 CE2 PHE A1104 235.624 23.489 123.581 1.00 83.53 C ANISOU 2481 CE2 PHE A1104 12011 9894 9834 -1236 284 305 C ATOM 2482 CZ PHE A1104 235.241 23.705 124.889 1.00 86.57 C ANISOU 2482 CZ PHE A1104 12331 10505 10056 -1347 316 216 C ATOM 2483 N GLN A1105 241.604 25.324 125.626 1.00 81.70 N ANISOU 2483 N GLN A1105 12146 9105 9792 -1197 59 544 N ATOM 2484 CA GLN A1105 242.040 25.553 126.998 1.00 85.90 C ANISOU 2484 CA GLN A1105 12697 9710 10230 -1285 49 536 C ATOM 2485 C GLN A1105 242.556 26.972 127.204 1.00 82.64 C ANISOU 2485 C GLN A1105 12305 9250 9845 -1198 43 444 C ATOM 2486 O GLN A1105 242.318 27.575 128.258 1.00 89.92 O ANISOU 2486 O GLN A1105 13206 10280 10678 -1224 59 354 O ATOM 2487 CB GLN A1105 243.120 24.542 127.385 1.00 87.15 C ANISOU 2487 CB GLN A1105 12927 9796 10390 -1379 -29 679 C ATOM 2488 CG GLN A1105 243.669 24.749 128.787 1.00 92.19 C ANISOU 2488 CG GLN A1105 13599 10497 10934 -1477 -51 685 C ATOM 2489 CD GLN A1105 244.709 23.720 129.170 1.00 93.33 C ANISOU 2489 CD GLN A1105 13824 10555 11081 -1553 -160 816 C ATOM 2490 OE1 GLN A1105 244.407 22.536 129.304 1.00 97.26 O ANISOU 2490 OE1 GLN A1105 14368 11051 11536 -1654 -224 905 O ATOM 2491 NE2 GLN A1105 245.940 24.170 129.368 1.00 92.42 N ANISOU 2491 NE2 GLN A1105 13735 10366 11012 -1509 -201 821 N ATOM 2492 N MET A1106 243.259 27.524 126.219 1.00 77.28 N ANISOU 2492 N MET A1106 11671 8419 9272 -1111 9 463 N ATOM 2493 CA MET A1106 243.950 28.794 126.393 1.00 77.67 C ANISOU 2493 CA MET A1106 11779 8396 9338 -1070 -27 411 C ATOM 2494 C MET A1106 243.311 29.952 125.649 1.00 78.57 C ANISOU 2494 C MET A1106 11920 8437 9496 -951 -54 302 C ATOM 2495 O MET A1106 243.446 31.096 126.087 1.00 80.33 O ANISOU 2495 O MET A1106 12199 8620 9702 -912 -103 216 O ATOM 2496 CB MET A1106 245.409 28.665 125.943 1.00 78.97 C ANISOU 2496 CB MET A1106 11990 8461 9555 -1107 -70 514 C ATOM 2497 CG MET A1106 246.136 27.483 126.561 1.00 84.36 C ANISOU 2497 CG MET A1106 12658 9182 10212 -1189 -87 609 C ATOM 2498 SD MET A1106 247.835 27.347 125.983 1.00 82.18 S ANISOU 2498 SD MET A1106 12391 8844 9991 -1200 -147 672 S ATOM 2499 CE MET A1106 248.506 28.908 126.553 1.00 83.36 C ANISOU 2499 CE MET A1106 12601 8974 10097 -1231 -158 620 C ATOM 2500 N GLY A1107 242.628 29.692 124.542 1.00 77.88 N ANISOU 2500 N GLY A1107 11809 8318 9465 -891 -45 303 N ATOM 2501 CA GLY A1107 242.041 30.746 123.740 1.00 78.61 C ANISOU 2501 CA GLY A1107 11950 8314 9605 -776 -103 209 C ATOM 2502 C GLY A1107 242.832 30.999 122.472 1.00 79.77 C ANISOU 2502 C GLY A1107 12179 8308 9822 -797 -155 306 C ATOM 2503 O GLY A1107 243.899 30.426 122.230 1.00 80.85 O ANISOU 2503 O GLY A1107 12313 8439 9968 -889 -138 421 O ATOM 2504 N GLU A1108 242.278 31.887 121.644 1.00 81.81 N ANISOU 2504 N GLU A1108 12509 8456 10119 -713 -233 244 N ATOM 2505 CA GLU A1108 242.924 32.218 120.379 1.00 80.91 C ANISOU 2505 CA GLU A1108 12484 8213 10045 -767 -293 336 C ATOM 2506 C GLU A1108 244.236 32.960 120.605 1.00 83.64 C ANISOU 2506 C GLU A1108 12934 8491 10352 -884 -357 395 C ATOM 2507 O GLU A1108 245.235 32.680 119.934 1.00 83.05 O ANISOU 2507 O GLU A1108 12859 8427 10270 -1003 -346 499 O ATOM 2508 CB GLU A1108 241.978 33.046 119.509 1.00 82.26 C ANISOU 2508 CB GLU A1108 12739 8262 10255 -661 -395 260 C ATOM 2509 CG GLU A1108 242.585 33.514 118.198 1.00 81.07 C ANISOU 2509 CG GLU A1108 12706 7978 10119 -754 -479 361 C ATOM 2510 CD GLU A1108 241.626 34.352 117.376 1.00 82.98 C ANISOU 2510 CD GLU A1108 13060 8070 10396 -649 -616 291 C ATOM 2511 OE1 GLU A1108 240.405 34.282 117.629 1.00 82.16 O ANISOU 2511 OE1 GLU A1108 12890 8004 10322 -482 -612 157 O ATOM 2512 OE2 GLU A1108 242.094 35.081 116.476 1.00 84.50 O ANISOU 2512 OE2 GLU A1108 13409 8120 10576 -746 -739 364 O ATOM 2513 N THR A1109 244.255 33.899 121.554 1.00 85.45 N ANISOU 2513 N THR A1109 13243 8677 10547 -856 -426 314 N ATOM 2514 CA THR A1109 245.466 34.673 121.813 1.00 84.45 C ANISOU 2514 CA THR A1109 13229 8485 10373 -980 -496 368 C ATOM 2515 C THR A1109 246.533 33.828 122.500 1.00 84.13 C ANISOU 2515 C THR A1109 13087 8582 10297 -1083 -395 443 C ATOM 2516 O THR A1109 247.709 33.879 122.123 1.00 84.12 O ANISOU 2516 O THR A1109 13105 8593 10262 -1218 -407 528 O ATOM 2517 CB THR A1109 245.133 35.901 122.661 1.00 88.05 C ANISOU 2517 CB THR A1109 13804 8844 10807 -905 -614 246 C ATOM 2518 OG1 THR A1109 244.250 36.762 121.933 1.00 88.76 O ANISOU 2518 OG1 THR A1109 14016 8773 10935 -797 -759 166 O ATOM 2519 CG2 THR A1109 246.398 36.668 123.013 1.00 86.50 C ANISOU 2519 CG2 THR A1109 13731 8584 10551 -1053 -687 309 C ATOM 2520 N GLY A1110 246.142 33.050 123.512 1.00 82.18 N ANISOU 2520 N GLY A1110 12730 8451 10042 -1030 -310 406 N ATOM 2521 CA GLY A1110 247.118 32.252 124.239 1.00 79.83 C ANISOU 2521 CA GLY A1110 12362 8257 9713 -1114 -251 472 C ATOM 2522 C GLY A1110 247.841 31.254 123.354 1.00 77.13 C ANISOU 2522 C GLY A1110 11944 7962 9399 -1169 -218 565 C ATOM 2523 O GLY A1110 249.042 31.024 123.515 1.00 78.98 O ANISOU 2523 O GLY A1110 12153 8250 9607 -1251 -223 610 O ATOM 2524 N VAL A1111 247.123 30.654 122.405 1.00 72.71 N ANISOU 2524 N VAL A1111 11339 7398 8891 -1115 -191 575 N ATOM 2525 CA VAL A1111 247.748 29.699 121.496 1.00 66.95 C ANISOU 2525 CA VAL A1111 10528 6720 8191 -1146 -170 636 C ATOM 2526 C VAL A1111 248.543 30.422 120.417 1.00 66.17 C ANISOU 2526 C VAL A1111 10467 6604 8070 -1239 -213 661 C ATOM 2527 O VAL A1111 249.647 30.001 120.056 1.00 66.28 O ANISOU 2527 O VAL A1111 10407 6715 8061 -1311 -211 682 O ATOM 2528 CB VAL A1111 246.685 28.764 120.896 1.00 66.19 C ANISOU 2528 CB VAL A1111 10370 6629 8150 -1065 -129 637 C ATOM 2529 CG1 VAL A1111 247.294 27.881 119.818 1.00 65.71 C ANISOU 2529 CG1 VAL A1111 10229 6612 8124 -1079 -126 676 C ATOM 2530 CG2 VAL A1111 246.070 27.916 121.989 1.00 66.83 C ANISOU 2530 CG2 VAL A1111 10413 6763 8216 -1036 -96 631 C ATOM 2531 N ALA A1112 248.006 31.524 119.890 1.00 66.12 N ANISOU 2531 N ALA A1112 10578 6488 8057 -1249 -269 649 N ATOM 2532 CA ALA A1112 248.770 32.338 118.955 1.00 65.98 C ANISOU 2532 CA ALA A1112 10635 6450 7984 -1394 -333 691 C ATOM 2533 C ALA A1112 249.988 32.981 119.605 1.00 66.95 C ANISOU 2533 C ALA A1112 10802 6613 8022 -1529 -370 706 C ATOM 2534 O ALA A1112 250.855 33.488 118.886 1.00 67.04 O ANISOU 2534 O ALA A1112 10846 6671 7955 -1700 -413 747 O ATOM 2535 CB ALA A1112 247.878 33.416 118.336 1.00 65.95 C ANISOU 2535 CB ALA A1112 10792 6276 7988 -1377 -432 680 C ATOM 2536 N GLY A1113 250.067 32.982 120.938 1.00 69.85 N ANISOU 2536 N GLY A1113 11169 6984 8389 -1477 -356 674 N ATOM 2537 CA GLY A1113 251.301 33.385 121.592 1.00 72.72 C ANISOU 2537 CA GLY A1113 11543 7413 8674 -1600 -377 687 C ATOM 2538 C GLY A1113 252.458 32.472 121.234 1.00 70.57 C ANISOU 2538 C GLY A1113 11110 7329 8373 -1669 -329 701 C ATOM 2539 O GLY A1113 253.583 32.931 121.024 1.00 70.30 O ANISOU 2539 O GLY A1113 11070 7394 8247 -1829 -355 713 O ATOM 2540 N PHE A1114 252.198 31.166 121.175 1.00 71.26 N ANISOU 2540 N PHE A1114 11066 7480 8531 -1550 -273 684 N ATOM 2541 CA PHE A1114 253.127 30.227 120.567 1.00 73.81 C ANISOU 2541 CA PHE A1114 11228 7973 8845 -1569 -256 662 C ATOM 2542 C PHE A1114 253.354 30.649 119.125 1.00 76.92 C ANISOU 2542 C PHE A1114 11608 8431 9187 -1690 -264 671 C ATOM 2543 O PHE A1114 252.441 30.588 118.298 1.00 82.30 O ANISOU 2543 O PHE A1114 12321 9034 9916 -1648 -254 691 O ATOM 2544 CB PHE A1114 252.588 28.790 120.635 1.00 72.73 C ANISOU 2544 CB PHE A1114 10997 7836 8801 -1409 -234 645 C ATOM 2545 CG PHE A1114 252.173 28.340 122.026 1.00 71.35 C ANISOU 2545 CG PHE A1114 10860 7594 8655 -1327 -237 656 C ATOM 2546 CD1 PHE A1114 253.122 28.026 122.984 1.00 71.07 C ANISOU 2546 CD1 PHE A1114 10789 7623 8590 -1338 -273 640 C ATOM 2547 CD2 PHE A1114 250.835 28.215 122.364 1.00 73.41 C ANISOU 2547 CD2 PHE A1114 11183 7753 8957 -1256 -210 674 C ATOM 2548 CE1 PHE A1114 252.754 27.606 124.251 1.00 70.56 C ANISOU 2548 CE1 PHE A1114 10771 7507 8533 -1295 -286 661 C ATOM 2549 CE2 PHE A1114 250.459 27.794 123.634 1.00 74.64 C ANISOU 2549 CE2 PHE A1114 11364 7890 9106 -1225 -211 684 C ATOM 2550 CZ PHE A1114 251.423 27.490 124.576 1.00 71.45 C ANISOU 2550 CZ PHE A1114 10944 7536 8669 -1254 -252 687 C ATOM 2551 N THR A1115 254.553 31.117 118.818 1.00 75.77 N ANISOU 2551 N THR A1115 11419 8442 8929 -1863 -283 658 N ATOM 2552 CA THR A1115 254.846 31.573 117.470 1.00 75.36 C ANISOU 2552 CA THR A1115 11356 8490 8787 -2037 -295 672 C ATOM 2553 C THR A1115 255.942 30.773 116.784 1.00 80.21 C ANISOU 2553 C THR A1115 11736 9403 9339 -2088 -265 581 C ATOM 2554 O THR A1115 255.872 30.601 115.562 1.00 83.49 O ANISOU 2554 O THR A1115 12082 9921 9721 -2153 -251 568 O ATOM 2555 CB THR A1115 255.209 33.066 117.497 1.00 74.50 C ANISOU 2555 CB THR A1115 11429 8327 8553 -2268 -367 737 C ATOM 2556 OG1 THR A1115 254.114 33.797 118.068 1.00 72.35 O ANISOU 2556 OG1 THR A1115 11366 7772 8350 -2179 -420 784 O ATOM 2557 CG2 THR A1115 255.490 33.609 116.108 1.00 75.17 C ANISOU 2557 CG2 THR A1115 11537 8512 8513 -2505 -401 775 C ATOM 2558 N ASN A1116 256.902 30.225 117.528 1.00 81.73 N ANISOU 2558 N ASN A1116 11792 9744 9517 -2040 -265 500 N ATOM 2559 CA ASN A1116 257.935 29.366 116.971 1.00 84.70 C ANISOU 2559 CA ASN A1116 11917 10421 9846 -2031 -259 364 C ATOM 2560 C ASN A1116 257.438 27.948 116.733 1.00 86.01 C ANISOU 2560 C ASN A1116 11970 10557 10153 -1781 -262 295 C ATOM 2561 O ASN A1116 257.738 27.353 115.691 1.00 88.60 O ANISOU 2561 O ASN A1116 12129 11076 10460 -1770 -257 197 O ATOM 2562 CB ASN A1116 259.151 29.352 117.901 1.00 87.62 C ANISOU 2562 CB ASN A1116 12192 10952 10149 -2054 -286 286 C ATOM 2563 CG ASN A1116 260.004 30.577 117.723 1.00 87.08 C ANISOU 2563 CG ASN A1116 12154 11044 9890 -2356 -286 310 C ATOM 2564 OD1 ASN A1116 259.915 31.244 116.695 1.00 85.73 O ANISOU 2564 OD1 ASN A1116 12024 10935 9613 -2566 -277 357 O ATOM 2565 ND2 ASN A1116 260.812 30.905 118.725 1.00 88.46 N ANISOU 2565 ND2 ASN A1116 12325 11278 10008 -2403 -307 289 N ATOM 2566 N SER A1117 256.657 27.410 117.673 1.00 83.99 N ANISOU 2566 N SER A1117 11813 10072 10028 -1597 -280 345 N ATOM 2567 CA SER A1117 256.111 26.064 117.533 1.00 84.73 C ANISOU 2567 CA SER A1117 11845 10099 10247 -1383 -309 303 C ATOM 2568 C SER A1117 255.117 25.981 116.385 1.00 82.97 C ANISOU 2568 C SER A1117 11647 9813 10067 -1378 -265 343 C ATOM 2569 O SER A1117 255.026 24.948 115.713 1.00 84.96 O ANISOU 2569 O SER A1117 11784 10118 10378 -1258 -288 269 O ATOM 2570 CB SER A1117 255.441 25.647 118.837 1.00 81.82 C ANISOU 2570 CB SER A1117 11607 9512 9970 -1259 -340 373 C ATOM 2571 OG SER A1117 256.387 25.536 119.879 1.00 84.16 O ANISOU 2571 OG SER A1117 11873 9868 10236 -1245 -397 330 O ATOM 2572 N LEU A1118 254.337 27.041 116.169 1.00 83.21 N ANISOU 2572 N LEU A1118 11833 9712 10072 -1490 -222 452 N ATOM 2573 CA LEU A1118 253.391 27.027 115.059 1.00 87.91 C ANISOU 2573 CA LEU A1118 12457 10244 10702 -1488 -191 489 C ATOM 2574 C LEU A1118 254.120 26.992 113.723 1.00 87.35 C ANISOU 2574 C LEU A1118 12233 10416 10540 -1607 -180 415 C ATOM 2575 O LEU A1118 253.697 26.290 112.797 1.00 87.64 O ANISOU 2575 O LEU A1118 12190 10485 10625 -1535 -166 380 O ATOM 2576 CB LEU A1118 252.458 28.235 115.134 1.00 87.76 C ANISOU 2576 CB LEU A1118 12645 10029 10672 -1568 -184 598 C ATOM 2577 CG LEU A1118 251.410 28.220 116.249 1.00 85.30 C ANISOU 2577 CG LEU A1118 12456 9505 10448 -1435 -182 643 C ATOM 2578 CD1 LEU A1118 250.507 29.440 116.138 1.00 85.44 C ANISOU 2578 CD1 LEU A1118 12654 9355 10454 -1485 -202 702 C ATOM 2579 CD2 LEU A1118 250.599 26.931 116.218 1.00 81.48 C ANISOU 2579 CD2 LEU A1118 11913 8975 10071 -1264 -163 629 C ATOM 2580 N ARG A1119 255.221 27.736 113.605 1.00 86.62 N ANISOU 2580 N ARG A1119 12091 10519 10300 -1806 -186 385 N ATOM 2581 CA ARG A1119 256.042 27.634 112.403 1.00 87.33 C ANISOU 2581 CA ARG A1119 11995 10919 10269 -1947 -171 287 C ATOM 2582 C ARG A1119 256.679 26.255 112.294 1.00 89.75 C ANISOU 2582 C ARG A1119 12051 11423 10626 -1756 -192 103 C ATOM 2583 O ARG A1119 256.837 25.725 111.189 1.00 90.94 O ANISOU 2583 O ARG A1119 12037 11769 10748 -1755 -180 1 O ATOM 2584 CB ARG A1119 257.109 28.725 112.399 1.00 95.07 C ANISOU 2584 CB ARG A1119 12974 12097 11052 -2236 -179 291 C ATOM 2585 CG ARG A1119 256.547 30.131 112.493 1.00 98.51 C ANISOU 2585 CG ARG A1119 13688 12310 11431 -2429 -207 465 C ATOM 2586 CD ARG A1119 257.654 31.169 112.442 1.00104.01 C ANISOU 2586 CD ARG A1119 14399 13209 11913 -2751 -234 478 C ATOM 2587 NE ARG A1119 258.097 31.429 111.077 1.00105.42 N ANISOU 2587 NE ARG A1119 14486 13656 11912 -3021 -227 458 N ATOM 2588 CZ ARG A1119 259.280 31.946 110.764 1.00105.65 C ANISOU 2588 CZ ARG A1119 14413 14015 11712 -3326 -232 413 C ATOM 2589 NH1 ARG A1119 260.143 32.257 111.723 1.00105.03 N ANISOU 2589 NH1 ARG A1119 14313 14022 11570 -3380 -244 380 N ATOM 2590 NH2 ARG A1119 259.602 32.149 109.493 1.00107.02 N ANISOU 2590 NH2 ARG A1119 14501 14457 11704 -3597 -223 396 N ATOM 2591 N MET A1120 257.048 25.659 113.431 1.00 91.24 N ANISOU 2591 N MET A1120 12217 11561 10889 -1587 -242 51 N ATOM 2592 CA MET A1120 257.551 24.289 113.420 1.00 93.80 C ANISOU 2592 CA MET A1120 12348 12004 11287 -1362 -315 -126 C ATOM 2593 C MET A1120 256.461 23.311 113.002 1.00 93.61 C ANISOU 2593 C MET A1120 12367 11790 11412 -1173 -334 -103 C ATOM 2594 O MET A1120 256.719 22.372 112.240 1.00 95.16 O ANISOU 2594 O MET A1120 12391 12130 11636 -1051 -380 -255 O ATOM 2595 CB MET A1120 258.099 23.918 114.797 1.00 94.65 C ANISOU 2595 CB MET A1120 12473 12046 11441 -1235 -395 -159 C ATOM 2596 CG MET A1120 259.282 24.751 115.246 1.00 94.93 C ANISOU 2596 CG MET A1120 12440 12297 11331 -1403 -385 -207 C ATOM 2597 SD MET A1120 259.677 24.472 116.980 1.00 95.41 S ANISOU 2597 SD MET A1120 12584 12211 11457 -1269 -474 -195 S ATOM 2598 CE MET A1120 260.846 25.794 117.276 1.00 95.16 C ANISOU 2598 CE MET A1120 12507 12422 11228 -1542 -424 -207 C ATOM 2599 N LEU A1121 255.238 23.512 113.498 1.00 90.57 N ANISOU 2599 N LEU A1121 12199 11098 11115 -1145 -307 69 N ATOM 2600 CA LEU A1121 254.121 22.683 113.061 1.00 88.78 C ANISOU 2600 CA LEU A1121 12020 10704 11007 -1007 -314 106 C ATOM 2601 C LEU A1121 253.799 22.914 111.593 1.00 88.99 C ANISOU 2601 C LEU A1121 11980 10840 10992 -1097 -250 94 C ATOM 2602 O LEU A1121 253.335 21.995 110.908 1.00 89.79 O ANISOU 2602 O LEU A1121 12021 10924 11169 -973 -271 44 O ATOM 2603 CB LEU A1121 252.889 22.962 113.921 1.00 84.23 C ANISOU 2603 CB LEU A1121 11666 9838 10501 -989 -287 273 C ATOM 2604 CG LEU A1121 252.953 22.522 115.382 1.00 83.70 C ANISOU 2604 CG LEU A1121 11681 9641 10479 -900 -356 301 C ATOM 2605 CD1 LEU A1121 251.766 23.072 116.151 1.00 79.23 C ANISOU 2605 CD1 LEU A1121 11302 8868 9935 -935 -303 443 C ATOM 2606 CD2 LEU A1121 252.995 21.008 115.475 1.00 85.44 C ANISOU 2606 CD2 LEU A1121 11854 9818 10790 -716 -477 228 C ATOM 2607 N ASN A1122 254.039 24.128 111.093 1.00 90.51 N ANISOU 2607 N ASN A1122 12197 11136 11057 -1326 -187 144 N ATOM 2608 CA ASN A1122 253.760 24.420 109.691 1.00 92.60 C ANISOU 2608 CA ASN A1122 12417 11508 11259 -1451 -140 148 C ATOM 2609 C ASN A1122 254.736 23.697 108.772 1.00 91.83 C ANISOU 2609 C ASN A1122 12046 11752 11094 -1442 -154 -52 C ATOM 2610 O ASN A1122 254.351 23.225 107.696 1.00 91.40 O ANISOU 2610 O ASN A1122 11910 11763 11054 -1416 -136 -97 O ATOM 2611 CB ASN A1122 253.810 25.927 109.453 1.00 95.68 C ANISOU 2611 CB ASN A1122 12941 11901 11511 -1727 -110 266 C ATOM 2612 CG ASN A1122 253.419 26.305 108.043 1.00 98.11 C ANISOU 2612 CG ASN A1122 13251 12282 11746 -1883 -83 302 C ATOM 2613 OD1 ASN A1122 252.245 26.527 107.751 1.00 97.37 O ANISOU 2613 OD1 ASN A1122 13312 11958 11726 -1848 -78 412 O ATOM 2614 ND2 ASN A1122 254.405 26.378 107.155 1.00 99.94 N ANISOU 2614 ND2 ASN A1122 13300 12855 11816 -2067 -69 199 N ATOM 2615 N ASN A1123 256.001 23.602 109.178 1.00 94.29 N ANISOU 2615 N ASN A1123 12199 12302 11324 -1456 -189 -193 N ATOM 2616 CA ASN A1123 257.013 22.889 108.410 1.00 96.10 C ANISOU 2616 CA ASN A1123 12130 12904 11480 -1419 -218 -438 C ATOM 2617 C ASN A1123 256.936 21.380 108.589 1.00 96.33 C ANISOU 2617 C ASN A1123 12064 12865 11673 -1084 -325 -588 C ATOM 2618 O ASN A1123 257.802 20.669 108.069 1.00 99.55 O ANISOU 2618 O ASN A1123 12213 13571 12042 -987 -384 -836 O ATOM 2619 CB ASN A1123 258.412 23.377 108.800 1.00 98.99 C ANISOU 2619 CB ASN A1123 12345 13581 11685 -1557 -228 -559 C ATOM 2620 CG ASN A1123 258.614 24.852 108.518 1.00 99.82 C ANISOU 2620 CG ASN A1123 12546 13784 11597 -1929 -151 -422 C ATOM 2621 OD1 ASN A1123 257.905 25.444 107.705 1.00 99.11 O ANISOU 2621 OD1 ASN A1123 12575 13620 11463 -2098 -103 -288 O ATOM 2622 ND2 ASN A1123 259.591 25.454 109.189 1.00101.18 N ANISOU 2622 ND2 ASN A1123 12683 14113 11648 -2066 -159 -452 N ATOM 2623 N LYS A1124 255.931 20.883 109.312 1.00 96.07 N ANISOU 2623 N LYS A1124 12234 12459 11808 -915 -367 -454 N ATOM 2624 CA LYS A1124 255.747 19.453 109.554 1.00 97.23 C ANISOU 2624 CA LYS A1124 12358 12478 12107 -625 -502 -556 C ATOM 2625 C LYS A1124 256.956 18.831 110.247 1.00 97.70 C ANISOU 2625 C LYS A1124 12277 12675 12168 -470 -645 -756 C ATOM 2626 O LYS A1124 257.288 17.668 110.013 1.00 97.40 O ANISOU 2626 O LYS A1124 12117 12685 12204 -240 -792 -951 O ATOM 2627 CB LYS A1124 255.421 18.707 108.256 1.00 97.21 C ANISOU 2627 CB LYS A1124 12226 12573 12137 -541 -512 -669 C ATOM 2628 CG LYS A1124 254.123 19.164 107.608 1.00 96.32 C ANISOU 2628 CG LYS A1124 12265 12288 12045 -656 -396 -474 C ATOM 2629 CD LYS A1124 253.759 18.314 106.404 1.00 96.70 C ANISOU 2629 CD LYS A1124 12195 12408 12138 -554 -415 -582 C ATOM 2630 CE LYS A1124 252.429 18.754 105.814 1.00 97.17 C ANISOU 2630 CE LYS A1124 12413 12283 12225 -657 -309 -386 C ATOM 2631 NZ LYS A1124 252.023 17.912 104.656 1.00 98.22 N ANISOU 2631 NZ LYS A1124 12440 12474 12404 -560 -326 -482 N ATOM 2632 N ARG A1125 257.619 19.603 111.107 1.00 97.94 N ANISOU 2632 N ARG A1125 12332 12763 12119 -583 -622 -720 N ATOM 2633 CA ARG A1125 258.728 19.111 111.925 1.00 98.10 C ANISOU 2633 CA ARG A1125 12245 12888 12140 -440 -762 -890 C ATOM 2634 C ARG A1125 258.158 18.794 113.302 1.00 97.71 C ANISOU 2634 C ARG A1125 12451 12463 12211 -339 -847 -724 C ATOM 2635 O ARG A1125 258.093 19.651 114.183 1.00 97.62 O ANISOU 2635 O ARG A1125 12577 12357 12158 -478 -778 -570 O ATOM 2636 CB ARG A1125 259.855 20.133 111.998 1.00 98.20 C ANISOU 2636 CB ARG A1125 12113 13227 11972 -648 -684 -962 C ATOM 2637 CG ARG A1125 260.387 20.551 110.644 1.00 98.24 C ANISOU 2637 CG ARG A1125 11875 13639 11812 -824 -589 -1104 C ATOM 2638 CD ARG A1125 261.888 20.361 110.568 1.00104.81 C ANISOU 2638 CD ARG A1125 12392 14912 12518 -795 -655 -1407 C ATOM 2639 NE ARG A1125 262.247 19.090 109.947 1.00110.29 N ANISOU 2639 NE ARG A1125 12852 15774 13278 -515 -794 -1704 N ATOM 2640 CZ ARG A1125 263.472 18.574 109.962 1.00114.21 C ANISOU 2640 CZ ARG A1125 13060 16620 13716 -369 -913 -2032 C ATOM 2641 NH1 ARG A1125 264.458 19.220 110.568 1.00114.03 N ANISOU 2641 NH1 ARG A1125 12941 16827 13559 -497 -894 -2092 N ATOM 2642 NH2 ARG A1125 263.710 17.411 109.370 1.00117.97 N ANISOU 2642 NH2 ARG A1125 13337 17221 14264 -85 -1064 -2318 N ATOM 2643 N TRP A1126 257.745 17.541 113.484 1.00 96.98 N ANISOU 2643 N TRP A1126 12428 12162 12256 -110 -1012 -759 N ATOM 2644 CA TRP A1126 256.992 17.180 114.677 1.00 95.87 C ANISOU 2644 CA TRP A1126 12554 11665 12209 -64 -1091 -571 C ATOM 2645 C TRP A1126 257.892 17.024 115.896 1.00 96.37 C ANISOU 2645 C TRP A1126 12636 11713 12265 7 -1230 -625 C ATOM 2646 O TRP A1126 257.556 17.509 116.982 1.00 95.65 O ANISOU 2646 O TRP A1126 12726 11454 12163 -96 -1192 -446 O ATOM 2647 CB TRP A1126 256.207 15.896 114.418 1.00 95.28 C ANISOU 2647 CB TRP A1126 12576 11365 12261 111 -1238 -569 C ATOM 2648 CG TRP A1126 255.508 15.902 113.094 1.00 95.30 C ANISOU 2648 CG TRP A1126 12512 11427 12272 77 -1125 -570 C ATOM 2649 CD1 TRP A1126 255.697 15.026 112.065 1.00 96.53 C ANISOU 2649 CD1 TRP A1126 12519 11686 12472 236 -1223 -761 C ATOM 2650 CD2 TRP A1126 254.524 16.842 112.644 1.00 94.59 C ANISOU 2650 CD2 TRP A1126 12499 11300 12142 -119 -908 -385 C ATOM 2651 NE1 TRP A1126 254.884 15.354 111.009 1.00 95.75 N ANISOU 2651 NE1 TRP A1126 12401 11621 12360 134 -1065 -690 N ATOM 2652 CE2 TRP A1126 254.155 16.465 111.338 1.00 94.84 C ANISOU 2652 CE2 TRP A1126 12427 11413 12194 -81 -879 -459 C ATOM 2653 CE3 TRP A1126 253.916 17.961 113.221 1.00 93.14 C ANISOU 2653 CE3 TRP A1126 12461 11018 11908 -307 -756 -182 C ATOM 2654 CZ2 TRP A1126 253.205 17.167 110.600 1.00 94.10 C ANISOU 2654 CZ2 TRP A1126 12383 11298 12075 -231 -706 -323 C ATOM 2655 CZ3 TRP A1126 252.976 18.657 112.486 1.00 92.46 C ANISOU 2655 CZ3 TRP A1126 12422 10906 11802 -435 -601 -66 C ATOM 2656 CH2 TRP A1126 252.630 18.258 111.189 1.00 92.38 C ANISOU 2656 CH2 TRP A1126 12317 10971 11814 -400 -577 -130 C ATOM 2657 N ASP A1127 259.035 16.354 115.739 1.00 97.31 N ANISOU 2657 N ASP A1127 12565 12021 12388 188 -1401 -887 N ATOM 2658 CA ASP A1127 259.936 16.163 116.871 1.00 98.18 C ANISOU 2658 CA ASP A1127 12688 12121 12496 276 -1559 -957 C ATOM 2659 C ASP A1127 260.510 17.485 117.363 1.00 97.58 C ANISOU 2659 C ASP A1127 12565 12223 12289 59 -1386 -897 C ATOM 2660 O ASP A1127 260.737 17.649 118.567 1.00 97.28 O ANISOU 2660 O ASP A1127 12651 12064 12248 40 -1441 -814 O ATOM 2661 CB ASP A1127 261.061 15.201 116.492 1.00104.42 C ANISOU 2661 CB ASP A1127 13253 13110 13314 542 -1793 -1297 C ATOM 2662 CG ASP A1127 260.546 13.922 115.859 1.00107.01 C ANISOU 2662 CG ASP A1127 13619 13274 13768 765 -1982 -1386 C ATOM 2663 OD1 ASP A1127 259.403 13.524 116.166 1.00103.65 O ANISOU 2663 OD1 ASP A1127 13458 12501 13423 737 -2008 -1160 O ATOM 2664 OD2 ASP A1127 261.285 13.313 115.057 1.00109.88 O ANISOU 2664 OD2 ASP A1127 13739 13871 14139 962 -2110 -1693 O ATOM 2665 N GLU A1128 260.747 18.434 116.457 1.00 97.90 N ANISOU 2665 N GLU A1128 12443 12544 12210 -124 -1191 -932 N ATOM 2666 CA GLU A1128 261.245 19.742 116.869 1.00 98.54 C ANISOU 2666 CA GLU A1128 12511 12775 12155 -362 -1041 -858 C ATOM 2667 C GLU A1128 260.181 20.517 117.637 1.00 97.91 C ANISOU 2667 C GLU A1128 12715 12392 12095 -519 -924 -559 C ATOM 2668 O GLU A1128 260.463 21.106 118.687 1.00 97.72 O ANISOU 2668 O GLU A1128 12783 12316 12031 -601 -911 -476 O ATOM 2669 CB GLU A1128 261.716 20.532 115.647 1.00 99.03 C ANISOU 2669 CB GLU A1128 12360 13204 12065 -557 -890 -955 C ATOM 2670 CG GLU A1128 262.844 19.873 114.871 1.00 99.02 C ANISOU 2670 CG GLU A1128 12023 13594 12005 -426 -986 -1293 C ATOM 2671 CD GLU A1128 263.423 20.783 113.802 1.00 99.04 C ANISOU 2671 CD GLU A1128 11809 14019 11802 -695 -828 -1379 C ATOM 2672 OE1 GLU A1128 263.194 22.009 113.877 1.00100.53 O ANISOU 2672 OE1 GLU A1128 12126 14187 11885 -989 -677 -1177 O ATOM 2673 OE2 GLU A1128 264.110 20.273 112.890 1.00103.16 O ANISOU 2673 OE2 GLU A1128 12037 14901 12258 -621 -870 -1657 O ATOM 2674 N ALA A1129 258.945 20.524 117.128 1.00 97.01 N ANISOU 2674 N ALA A1129 12730 12092 12039 -553 -844 -413 N ATOM 2675 CA ALA A1129 257.869 21.244 117.801 1.00 95.00 C ANISOU 2675 CA ALA A1129 12715 11582 11798 -679 -741 -171 C ATOM 2676 C ALA A1129 257.480 20.581 119.115 1.00 93.65 C ANISOU 2676 C ALA A1129 12720 11156 11709 -576 -857 -81 C ATOM 2677 O ALA A1129 257.053 21.267 120.051 1.00 92.02 O ANISOU 2677 O ALA A1129 12665 10822 11477 -683 -793 65 O ATOM 2678 CB ALA A1129 256.651 21.348 116.885 1.00 93.36 C ANISOU 2678 CB ALA A1129 12577 11267 11628 -721 -642 -70 C ATOM 2679 N ALA A1130 257.615 19.255 119.202 1.00 94.16 N ANISOU 2679 N ALA A1130 12773 11143 11860 -378 -1043 -170 N ATOM 2680 CA ALA A1130 257.258 18.549 120.427 1.00 92.88 C ANISOU 2680 CA ALA A1130 12803 10734 11754 -315 -1187 -72 C ATOM 2681 C ALA A1130 258.179 18.919 121.582 1.00 93.51 C ANISOU 2681 C ALA A1130 12892 10858 11780 -342 -1241 -88 C ATOM 2682 O ALA A1130 257.742 18.944 122.737 1.00 91.87 O ANISOU 2682 O ALA A1130 12865 10474 11568 -403 -1267 57 O ATOM 2683 CB ALA A1130 257.291 17.040 120.190 1.00 93.41 C ANISOU 2683 CB ALA A1130 12880 10690 11920 -102 -1424 -172 C ATOM 2684 N VAL A1131 259.448 19.206 121.294 1.00 95.17 N ANISOU 2684 N VAL A1131 12899 11328 11934 -313 -1257 -269 N ATOM 2685 CA VAL A1131 260.388 19.547 122.354 1.00 95.64 C ANISOU 2685 CA VAL A1131 12950 11450 11937 -335 -1312 -300 C ATOM 2686 C VAL A1131 260.177 20.979 122.824 1.00 95.12 C ANISOU 2686 C VAL A1131 12956 11407 11778 -569 -1108 -151 C ATOM 2687 O VAL A1131 260.202 21.258 124.027 1.00 94.49 O ANISOU 2687 O VAL A1131 13004 11222 11678 -623 -1126 -55 O ATOM 2688 CB VAL A1131 261.831 19.314 121.872 1.00 97.00 C ANISOU 2688 CB VAL A1131 12856 11930 12070 -218 -1410 -574 C ATOM 2689 CG1 VAL A1131 262.823 19.725 122.948 1.00 97.67 C ANISOU 2689 CG1 VAL A1131 12921 12101 12089 -249 -1459 -611 C ATOM 2690 CG2 VAL A1131 262.028 17.860 121.485 1.00 96.86 C ANISOU 2690 CG2 VAL A1131 12782 11863 12158 55 -1656 -750 C ATOM 2691 N ASN A1132 259.960 21.906 121.890 1.00 95.19 N ANISOU 2691 N ASN A1132 12899 11543 11725 -712 -932 -132 N ATOM 2692 CA ASN A1132 259.838 23.311 122.262 1.00 94.23 C ANISOU 2692 CA ASN A1132 12860 11432 11512 -926 -779 -12 C ATOM 2693 C ASN A1132 258.591 23.554 123.104 1.00 90.70 C ANISOU 2693 C ASN A1132 12644 10710 11108 -968 -731 181 C ATOM 2694 O ASN A1132 258.618 24.356 124.045 1.00 90.13 O ANISOU 2694 O ASN A1132 12669 10593 10984 -1071 -686 259 O ATOM 2695 CB ASN A1132 259.826 24.183 121.005 1.00 94.42 C ANISOU 2695 CB ASN A1132 12797 11621 11456 -1080 -645 -27 C ATOM 2696 CG ASN A1132 260.164 25.634 121.296 1.00 93.89 C ANISOU 2696 CG ASN A1132 12786 11621 11266 -1308 -547 44 C ATOM 2697 OD1 ASN A1132 259.545 26.272 122.146 1.00 97.19 O ANISOU 2697 OD1 ASN A1132 13388 11847 11693 -1367 -509 181 O ATOM 2698 ND2 ASN A1132 261.155 26.160 120.590 1.00 94.90 N ANISOU 2698 ND2 ASN A1132 12755 12038 11266 -1448 -517 -59 N ATOM 2699 N LEU A1133 257.491 22.864 122.790 1.00 88.45 N ANISOU 2699 N LEU A1133 12437 10264 10906 -893 -741 244 N ATOM 2700 CA LEU A1133 256.273 23.024 123.578 1.00 84.37 C ANISOU 2700 CA LEU A1133 12106 9541 10408 -941 -694 398 C ATOM 2701 C LEU A1133 256.437 22.480 124.991 1.00 83.68 C ANISOU 2701 C LEU A1133 12119 9355 10319 -915 -808 442 C ATOM 2702 O LEU A1133 255.793 22.975 125.923 1.00 81.06 O ANISOU 2702 O LEU A1133 11912 8937 9952 -1006 -751 545 O ATOM 2703 CB LEU A1133 255.098 22.338 122.881 1.00 83.52 C ANISOU 2703 CB LEU A1133 12042 9320 10372 -883 -685 445 C ATOM 2704 CG LEU A1133 254.570 23.036 121.629 1.00 82.94 C ANISOU 2704 CG LEU A1133 11923 9296 10293 -937 -556 446 C ATOM 2705 CD1 LEU A1133 253.488 22.200 120.969 1.00 79.68 C ANISOU 2705 CD1 LEU A1133 11539 8780 9956 -863 -563 479 C ATOM 2706 CD2 LEU A1133 254.048 24.419 121.979 1.00 81.94 C ANISOU 2706 CD2 LEU A1133 11893 9131 10110 -1069 -438 527 C ATOM 2707 N ALA A1134 257.291 21.472 125.173 1.00 86.02 N ANISOU 2707 N ALA A1134 12363 9670 10649 -791 -983 352 N ATOM 2708 CA ALA A1134 257.557 20.944 126.504 1.00 85.80 C ANISOU 2708 CA ALA A1134 12446 9542 10611 -777 -1125 396 C ATOM 2709 C ALA A1134 258.312 21.930 127.384 1.00 87.25 C ANISOU 2709 C ALA A1134 12619 9818 10715 -874 -1070 396 C ATOM 2710 O ALA A1134 258.461 21.675 128.583 1.00 91.31 O ANISOU 2710 O ALA A1134 13236 10253 11204 -895 -1163 450 O ATOM 2711 CB ALA A1134 258.340 19.634 126.402 1.00 88.32 C ANISOU 2711 CB ALA A1134 12722 9840 10994 -594 -1370 276 C ATOM 2712 N LYS A1135 258.788 23.039 126.821 1.00 87.67 N ANISOU 2712 N LYS A1135 12563 10033 10714 -953 -933 343 N ATOM 2713 CA LYS A1135 259.486 24.067 127.580 1.00 88.42 C ANISOU 2713 CA LYS A1135 12657 10215 10724 -1065 -878 346 C ATOM 2714 C LYS A1135 258.547 25.158 128.085 1.00 89.96 C ANISOU 2714 C LYS A1135 12988 10317 10877 -1205 -736 471 C ATOM 2715 O LYS A1135 258.875 25.842 129.063 1.00 91.89 O ANISOU 2715 O LYS A1135 13286 10569 11060 -1288 -717 500 O ATOM 2716 CB LYS A1135 260.604 24.661 126.707 1.00 91.51 C ANISOU 2716 CB LYS A1135 12864 10852 11054 -1104 -837 215 C ATOM 2717 CG LYS A1135 260.894 26.148 126.871 1.00 90.92 C ANISOU 2717 CG LYS A1135 12812 10860 10875 -1297 -711 253 C ATOM 2718 CD LYS A1135 261.814 26.414 128.053 1.00 92.23 C ANISOU 2718 CD LYS A1135 12982 11081 10981 -1332 -764 234 C ATOM 2719 CE LYS A1135 262.168 27.889 128.150 1.00 95.88 C ANISOU 2719 CE LYS A1135 13474 11625 11332 -1533 -659 267 C ATOM 2720 NZ LYS A1135 260.955 28.752 128.142 1.00 94.79 N ANISOU 2720 NZ LYS A1135 13507 11307 11203 -1619 -561 392 N ATOM 2721 N SER A1136 257.371 25.293 127.479 1.00 93.28 N ANISOU 2721 N SER A1136 13463 10651 11331 -1217 -652 530 N ATOM 2722 CA SER A1136 256.455 26.385 127.772 1.00 94.60 C ANISOU 2722 CA SER A1136 13734 10747 11462 -1316 -535 602 C ATOM 2723 C SER A1136 255.869 26.261 129.179 1.00 93.53 C ANISOU 2723 C SER A1136 13712 10525 11299 -1344 -549 670 C ATOM 2724 O SER A1136 255.985 25.232 129.851 1.00 95.33 O ANISOU 2724 O SER A1136 13967 10717 11538 -1307 -654 694 O ATOM 2725 CB SER A1136 255.326 26.412 126.745 1.00 93.22 C ANISOU 2725 CB SER A1136 13574 10512 11335 -1293 -465 625 C ATOM 2726 OG SER A1136 254.587 25.203 126.783 1.00 91.24 O ANISOU 2726 OG SER A1136 13345 10182 11141 -1213 -517 658 O ATOM 2727 N ARG A1137 255.222 27.346 129.618 1.00 88.69 N ANISOU 2727 N ARG A1137 13172 9884 10643 -1418 -460 692 N ATOM 2728 CA ARG A1137 254.495 27.327 130.883 1.00 86.08 C ANISOU 2728 CA ARG A1137 12925 9517 10265 -1460 -451 733 C ATOM 2729 C ARG A1137 253.296 26.391 130.815 1.00 82.27 C ANISOU 2729 C ARG A1137 12469 8987 9803 -1437 -453 777 C ATOM 2730 O ARG A1137 253.010 25.668 131.778 1.00 80.59 O ANISOU 2730 O ARG A1137 12309 8767 9545 -1485 -506 827 O ATOM 2731 CB ARG A1137 254.037 28.739 131.249 1.00 84.96 C ANISOU 2731 CB ARG A1137 12836 9370 10074 -1514 -369 704 C ATOM 2732 CG ARG A1137 255.142 29.663 131.726 1.00 85.82 C ANISOU 2732 CG ARG A1137 12957 9518 10132 -1577 -382 679 C ATOM 2733 CD ARG A1137 254.600 30.679 132.719 1.00 85.48 C ANISOU 2733 CD ARG A1137 12991 9459 10028 -1622 -345 652 C ATOM 2734 NE ARG A1137 254.129 30.046 133.948 1.00 85.39 N ANISOU 2734 NE ARG A1137 12993 9482 9968 -1646 -351 673 N ATOM 2735 CZ ARG A1137 254.905 29.769 134.991 1.00 85.36 C ANISOU 2735 CZ ARG A1137 13000 9520 9912 -1701 -399 699 C ATOM 2736 NH1 ARG A1137 254.390 29.192 136.068 1.00 85.87 N ANISOU 2736 NH1 ARG A1137 13091 9623 9913 -1756 -412 730 N ATOM 2737 NH2 ARG A1137 256.195 30.072 134.959 1.00 85.50 N ANISOU 2737 NH2 ARG A1137 12999 9560 9928 -1720 -440 693 N ATOM 2738 N TRP A1138 252.581 26.401 129.685 1.00 79.76 N ANISOU 2738 N TRP A1138 12123 8643 9540 -1387 -401 764 N ATOM 2739 CA TRP A1138 251.408 25.547 129.515 1.00 74.10 C ANISOU 2739 CA TRP A1138 11423 7896 8836 -1376 -397 801 C ATOM 2740 C TRP A1138 251.737 24.079 129.747 1.00 73.37 C ANISOU 2740 C TRP A1138 11356 7762 8758 -1368 -529 858 C ATOM 2741 O TRP A1138 250.893 23.325 130.245 1.00 73.16 O ANISOU 2741 O TRP A1138 11390 7718 8689 -1431 -559 918 O ATOM 2742 CB TRP A1138 250.823 25.753 128.116 1.00 73.70 C ANISOU 2742 CB TRP A1138 11329 7821 8852 -1310 -337 774 C ATOM 2743 CG TRP A1138 249.939 24.640 127.652 1.00 75.51 C ANISOU 2743 CG TRP A1138 11558 8018 9113 -1284 -356 812 C ATOM 2744 CD1 TRP A1138 248.648 24.418 128.017 1.00 78.71 C ANISOU 2744 CD1 TRP A1138 11989 8444 9471 -1331 -312 831 C ATOM 2745 CD2 TRP A1138 250.280 23.598 126.728 1.00 75.45 C ANISOU 2745 CD2 TRP A1138 11517 7971 9180 -1213 -431 822 C ATOM 2746 NE1 TRP A1138 248.161 23.300 127.384 1.00 78.66 N ANISOU 2746 NE1 TRP A1138 11985 8399 9504 -1312 -355 873 N ATOM 2747 CE2 TRP A1138 249.144 22.779 126.586 1.00 77.00 C ANISOU 2747 CE2 TRP A1138 11745 8136 9376 -1228 -435 867 C ATOM 2748 CE3 TRP A1138 251.435 23.278 126.009 1.00 75.49 C ANISOU 2748 CE3 TRP A1138 11454 7988 9241 -1139 -501 779 C ATOM 2749 CZ2 TRP A1138 249.128 21.661 125.756 1.00 76.68 C ANISOU 2749 CZ2 TRP A1138 11695 8038 9402 -1165 -516 883 C ATOM 2750 CZ3 TRP A1138 251.417 22.167 125.185 1.00 76.19 C ANISOU 2750 CZ3 TRP A1138 11513 8040 9398 -1057 -581 770 C ATOM 2751 CH2 TRP A1138 250.272 21.372 125.066 1.00 76.29 C ANISOU 2751 CH2 TRP A1138 11583 7984 9421 -1067 -593 828 C ATOM 2752 N TYR A1139 252.954 23.656 129.400 1.00 74.28 N ANISOU 2752 N TYR A1139 11429 7871 8922 -1297 -627 829 N ATOM 2753 CA TYR A1139 253.361 22.280 129.658 1.00 75.76 C ANISOU 2753 CA TYR A1139 11659 7992 9133 -1258 -805 859 C ATOM 2754 C TYR A1139 253.593 22.035 131.142 1.00 82.18 C ANISOU 2754 C TYR A1139 12573 8787 9864 -1353 -894 920 C ATOM 2755 O TYR A1139 253.348 20.927 131.633 1.00 87.11 O ANISOU 2755 O TYR A1139 13303 9326 10468 -1391 -1040 993 O ATOM 2756 CB TYR A1139 254.623 21.956 128.857 1.00 78.72 C ANISOU 2756 CB TYR A1139 11932 8399 9580 -1128 -897 763 C ATOM 2757 CG TYR A1139 255.151 20.549 129.035 1.00 84.37 C ANISOU 2757 CG TYR A1139 12691 9028 10337 -1037 -1127 753 C ATOM 2758 CD1 TYR A1139 254.729 19.518 128.206 1.00 87.28 C ANISOU 2758 CD1 TYR A1139 13071 9316 10776 -950 -1220 746 C ATOM 2759 CD2 TYR A1139 256.089 20.256 130.016 1.00 87.22 C ANISOU 2759 CD2 TYR A1139 13093 9377 10671 -1027 -1276 743 C ATOM 2760 CE1 TYR A1139 255.216 18.234 128.358 1.00 90.47 C ANISOU 2760 CE1 TYR A1139 13540 9610 11224 -849 -1475 725 C ATOM 2761 CE2 TYR A1139 256.582 18.976 130.175 1.00 90.38 C ANISOU 2761 CE2 TYR A1139 13556 9669 11114 -924 -1532 722 C ATOM 2762 CZ TYR A1139 256.142 17.969 129.344 1.00 92.68 C ANISOU 2762 CZ TYR A1139 13872 9864 11479 -831 -1641 710 C ATOM 2763 OH TYR A1139 256.634 16.694 129.501 1.00 96.75 O ANISOU 2763 OH TYR A1139 14475 10241 12042 -712 -1938 677 O ATOM 2764 N ASN A1140 254.061 23.051 131.870 1.00 86.13 N ANISOU 2764 N ASN A1140 13058 9358 10308 -1409 -822 899 N ATOM 2765 CA ASN A1140 254.308 22.897 133.299 1.00 89.27 C ANISOU 2765 CA ASN A1140 13545 9755 10618 -1510 -898 954 C ATOM 2766 C ASN A1140 253.014 22.939 134.105 1.00 89.85 C ANISOU 2766 C ASN A1140 13694 9858 10588 -1661 -828 1024 C ATOM 2767 O ASN A1140 252.897 22.242 135.119 1.00 89.30 O ANISOU 2767 O ASN A1140 13727 9769 10433 -1779 -936 1105 O ATOM 2768 CB ASN A1140 255.269 23.988 133.778 1.00 92.64 C ANISOU 2768 CB ASN A1140 13922 10260 11017 -1519 -844 897 C ATOM 2769 CG ASN A1140 255.973 23.626 135.073 1.00 98.10 C ANISOU 2769 CG ASN A1140 14686 10943 11643 -1580 -971 937 C ATOM 2770 OD1 ASN A1140 255.438 22.897 135.907 1.00103.38 O ANISOU 2770 OD1 ASN A1140 15467 11567 12247 -1679 -1055 1026 O ATOM 2771 ND2 ASN A1140 257.184 24.143 135.248 1.00 99.20 N ANISOU 2771 ND2 ASN A1140 14767 11138 11787 -1541 -992 874 N ATOM 2772 N GLN A1141 252.035 23.732 133.664 1.00 89.05 N ANISOU 2772 N GLN A1141 13538 9817 10478 -1669 -663 983 N ATOM 2773 CA GLN A1141 250.793 23.877 134.417 1.00 85.77 C ANISOU 2773 CA GLN A1141 13149 9492 9947 -1803 -583 1001 C ATOM 2774 C GLN A1141 249.973 22.590 134.390 1.00 84.64 C ANISOU 2774 C GLN A1141 13075 9322 9763 -1893 -665 1092 C ATOM 2775 O GLN A1141 249.459 22.149 135.425 1.00 85.15 O ANISOU 2775 O GLN A1141 13210 9454 9690 -2073 -702 1157 O ATOM 2776 CB GLN A1141 249.989 25.056 133.864 1.00 81.19 C ANISOU 2776 CB GLN A1141 12487 8980 9383 -1747 -419 900 C ATOM 2777 CG GLN A1141 248.652 25.283 134.543 1.00 80.49 C ANISOU 2777 CG GLN A1141 12378 9033 9171 -1853 -331 863 C ATOM 2778 CD GLN A1141 247.489 24.768 133.722 1.00 80.47 C ANISOU 2778 CD GLN A1141 12342 9049 9181 -1843 -290 862 C ATOM 2779 OE1 GLN A1141 247.634 24.475 132.535 1.00 80.60 O ANISOU 2779 OE1 GLN A1141 12349 8959 9316 -1733 -308 877 O ATOM 2780 NE2 GLN A1141 246.324 24.655 134.349 1.00 81.40 N ANISOU 2780 NE2 GLN A1141 12431 9332 9166 -1968 -233 834 N ATOM 2781 N THR A1142 249.839 21.970 133.218 1.00 83.40 N ANISOU 2781 N THR A1142 12905 9075 9707 -1793 -701 1100 N ATOM 2782 CA THR A1142 249.138 20.694 133.066 1.00 83.11 C ANISOU 2782 CA THR A1142 12954 8983 9642 -1874 -805 1191 C ATOM 2783 C THR A1142 250.073 19.704 132.388 1.00 84.53 C ANISOU 2783 C THR A1142 13182 8994 9941 -1743 -995 1212 C ATOM 2784 O THR A1142 250.008 19.503 131.167 1.00 86.49 O ANISOU 2784 O THR A1142 13371 9194 10298 -1611 -982 1169 O ATOM 2785 CB THR A1142 247.839 20.854 132.273 1.00 80.77 C ANISOU 2785 CB THR A1142 12588 8755 9345 -1874 -669 1158 C ATOM 2786 OG1 THR A1142 248.063 21.709 131.144 1.00 77.43 O ANISOU 2786 OG1 THR A1142 12056 8317 9048 -1693 -562 1060 O ATOM 2787 CG2 THR A1142 246.743 21.438 133.151 1.00 84.14 C ANISOU 2787 CG2 THR A1142 12978 9376 9614 -2032 -539 1128 C ATOM 2788 N PRO A1143 250.959 19.062 133.153 1.00 85.98 N ANISOU 2788 N PRO A1143 13470 9093 10105 -1767 -1190 1262 N ATOM 2789 CA PRO A1143 251.920 18.137 132.529 1.00 86.41 C ANISOU 2789 CA PRO A1143 13555 8997 10279 -1602 -1403 1236 C ATOM 2790 C PRO A1143 251.268 16.936 131.870 1.00 85.40 C ANISOU 2790 C PRO A1143 13519 8745 10184 -1599 -1538 1292 C ATOM 2791 O PRO A1143 251.673 16.550 130.767 1.00 87.72 O ANISOU 2791 O PRO A1143 13751 8974 10605 -1412 -1599 1212 O ATOM 2792 CB PRO A1143 252.814 17.722 133.707 1.00 90.16 C ANISOU 2792 CB PRO A1143 14150 9407 10701 -1653 -1605 1282 C ATOM 2793 CG PRO A1143 252.661 18.825 134.708 1.00 91.69 C ANISOU 2793 CG PRO A1143 14307 9749 10782 -1792 -1431 1292 C ATOM 2794 CD PRO A1143 251.233 19.264 134.584 1.00 88.86 C ANISOU 2794 CD PRO A1143 13911 9506 10347 -1919 -1230 1314 C ATOM 2795 N ASN A1144 250.264 16.334 132.511 1.00 84.25 N ANISOU 2795 N ASN A1144 13516 8583 9911 -1819 -1588 1422 N ATOM 2796 CA ASN A1144 249.675 15.111 131.974 1.00 85.89 C ANISOU 2796 CA ASN A1144 13848 8653 10133 -1849 -1752 1494 C ATOM 2797 C ASN A1144 248.939 15.370 130.664 1.00 83.52 C ANISOU 2797 C ASN A1144 13411 8408 9914 -1750 -1574 1428 C ATOM 2798 O ASN A1144 249.064 14.590 129.712 1.00 84.39 O ANISOU 2798 O ASN A1144 13540 8393 10132 -1614 -1699 1401 O ATOM 2799 CB ASN A1144 248.736 14.489 133.006 1.00 90.77 C ANISOU 2799 CB ASN A1144 14651 9282 10557 -2168 -1836 1657 C ATOM 2800 CG ASN A1144 249.465 14.030 134.249 1.00 95.64 C ANISOU 2800 CG ASN A1144 15446 9804 11087 -2284 -2069 1745 C ATOM 2801 OD1 ASN A1144 250.670 13.781 134.217 1.00 97.79 O ANISOU 2801 OD1 ASN A1144 15747 9937 11471 -2094 -2252 1689 O ATOM 2802 ND2 ASN A1144 248.738 13.915 135.354 1.00 95.83 N ANISOU 2802 ND2 ASN A1144 15584 9925 10901 -2604 -2069 1872 N ATOM 2803 N ARG A1145 248.168 16.457 130.594 1.00 81.22 N ANISOU 2803 N ARG A1145 12984 8300 9574 -1803 -1300 1390 N ATOM 2804 CA ARG A1145 247.419 16.749 129.376 1.00 78.39 C ANISOU 2804 CA ARG A1145 12507 7991 9287 -1715 -1141 1330 C ATOM 2805 C ARG A1145 248.338 17.212 128.253 1.00 76.44 C ANISOU 2805 C ARG A1145 12125 7716 9202 -1467 -1102 1208 C ATOM 2806 O ARG A1145 248.150 16.825 127.093 1.00 73.61 O ANISOU 2806 O ARG A1145 11722 7311 8936 -1356 -1108 1171 O ATOM 2807 CB ARG A1145 246.349 17.804 129.657 1.00 80.09 C ANISOU 2807 CB ARG A1145 12622 8405 9403 -1821 -897 1299 C ATOM 2808 CG ARG A1145 245.766 18.431 128.402 1.00 81.13 C ANISOU 2808 CG ARG A1145 12616 8585 9625 -1688 -728 1210 C ATOM 2809 CD ARG A1145 244.665 19.425 128.724 1.00 84.28 C ANISOU 2809 CD ARG A1145 12924 9172 9927 -1767 -530 1151 C ATOM 2810 NE ARG A1145 244.053 19.959 127.510 1.00 84.88 N ANISOU 2810 NE ARG A1145 12892 9270 10088 -1638 -405 1071 N ATOM 2811 CZ ARG A1145 242.939 20.686 127.488 1.00 86.29 C ANISOU 2811 CZ ARG A1145 12985 9594 10207 -1659 -261 994 C ATOM 2812 NH1 ARG A1145 242.308 20.970 128.618 1.00 86.43 N ANISOU 2812 NH1 ARG A1145 12987 9783 10071 -1806 -210 969 N ATOM 2813 NH2 ARG A1145 242.458 21.130 126.335 1.00 87.00 N ANISOU 2813 NH2 ARG A1145 12997 9674 10385 -1530 -180 926 N ATOM 2814 N ALA A1146 249.337 18.037 128.579 1.00 76.24 N ANISOU 2814 N ALA A1146 12032 7739 9197 -1399 -1063 1141 N ATOM 2815 CA ALA A1146 250.201 18.604 127.548 1.00 75.17 C ANISOU 2815 CA ALA A1146 11754 7633 9174 -1218 -1007 1023 C ATOM 2816 C ALA A1146 250.951 17.519 126.786 1.00 75.39 C ANISOU 2816 C ALA A1146 11779 7561 9304 -1063 -1203 970 C ATOM 2817 O ALA A1146 251.133 17.623 125.568 1.00 71.35 O ANISOU 2817 O ALA A1146 11149 7086 8876 -939 -1152 881 O ATOM 2818 CB ALA A1146 251.183 19.596 128.172 1.00 76.59 C ANISOU 2818 CB ALA A1146 11880 7890 9329 -1212 -958 972 C ATOM 2819 N LYS A1147 251.395 16.472 127.487 1.00 78.83 N ANISOU 2819 N LYS A1147 12348 7873 9729 -1066 -1446 1012 N ATOM 2820 CA LYS A1147 252.083 15.375 126.813 1.00 81.55 C ANISOU 2820 CA LYS A1147 12703 8108 10177 -888 -1678 933 C ATOM 2821 C LYS A1147 251.159 14.667 125.831 1.00 76.79 C ANISOU 2821 C LYS A1147 12124 7434 9620 -867 -1690 955 C ATOM 2822 O LYS A1147 251.587 14.271 124.741 1.00 75.86 O ANISOU 2822 O LYS A1147 11910 7311 9604 -687 -1751 835 O ATOM 2823 CB LYS A1147 252.634 14.384 127.840 1.00 83.69 C ANISOU 2823 CB LYS A1147 13157 8219 10422 -900 -1981 982 C ATOM 2824 CG LYS A1147 253.634 14.977 128.820 1.00 87.91 C ANISOU 2824 CG LYS A1147 13670 8818 10916 -907 -1997 953 C ATOM 2825 CD LYS A1147 254.152 13.912 129.778 1.00 90.47 C ANISOU 2825 CD LYS A1147 14198 8958 11218 -912 -2336 1004 C ATOM 2826 CE LYS A1147 254.910 14.524 130.946 1.00 94.92 C ANISOU 2826 CE LYS A1147 14768 9584 11712 -974 -2334 1015 C ATOM 2827 NZ LYS A1147 255.503 13.483 131.830 1.00 96.60 N ANISOU 2827 NZ LYS A1147 15187 9604 11910 -962 -2696 1056 N ATOM 2828 N ARG A1148 249.886 14.501 126.199 1.00 75.85 N ANISOU 2828 N ARG A1148 12120 7285 9415 -1056 -1630 1094 N ATOM 2829 CA ARG A1148 248.932 13.867 125.294 1.00 75.87 C ANISOU 2829 CA ARG A1148 12145 7233 9448 -1058 -1628 1123 C ATOM 2830 C ARG A1148 248.699 14.716 124.051 1.00 74.58 C ANISOU 2830 C ARG A1148 11782 7202 9354 -957 -1391 1027 C ATOM 2831 O ARG A1148 248.583 14.184 122.940 1.00 70.96 O ANISOU 2831 O ARG A1148 11278 6704 8979 -843 -1429 971 O ATOM 2832 CB ARG A1148 247.616 13.598 126.023 1.00 79.00 C ANISOU 2832 CB ARG A1148 12684 7626 9705 -1317 -1597 1282 C ATOM 2833 CG ARG A1148 247.698 12.459 127.027 1.00 83.89 C ANISOU 2833 CG ARG A1148 13550 8080 10244 -1457 -1889 1405 C ATOM 2834 CD ARG A1148 246.326 12.089 127.568 1.00 85.63 C ANISOU 2834 CD ARG A1148 13899 8337 10299 -1753 -1860 1559 C ATOM 2835 NE ARG A1148 245.755 13.156 128.384 1.00 85.01 N ANISOU 2835 NE ARG A1148 13733 8480 10085 -1924 -1615 1579 N ATOM 2836 CZ ARG A1148 245.920 13.259 129.699 1.00 82.74 C ANISOU 2836 CZ ARG A1148 13540 8234 9664 -2105 -1667 1653 C ATOM 2837 NH1 ARG A1148 246.638 12.354 130.352 1.00 81.60 N ANISOU 2837 NH1 ARG A1148 13598 7904 9501 -2148 -1965 1732 N ATOM 2838 NH2 ARG A1148 245.365 14.264 130.362 1.00 82.84 N ANISOU 2838 NH2 ARG A1148 13446 8471 9557 -2236 -1438 1636 N ATOM 2839 N VAL A1149 248.629 16.038 124.216 1.00 76.48 N ANISOU 2839 N VAL A1149 11915 7588 9555 -1002 -1164 1006 N ATOM 2840 CA VAL A1149 248.510 16.920 123.060 1.00 74.06 C ANISOU 2840 CA VAL A1149 11448 7386 9304 -921 -974 923 C ATOM 2841 C VAL A1149 249.800 16.909 122.248 1.00 75.73 C ANISOU 2841 C VAL A1149 11534 7637 9601 -751 -1035 788 C ATOM 2842 O VAL A1149 249.771 16.881 121.012 1.00 78.85 O ANISOU 2842 O VAL A1149 11825 8075 10059 -663 -989 716 O ATOM 2843 CB VAL A1149 248.135 18.342 123.515 1.00 70.55 C ANISOU 2843 CB VAL A1149 10958 7056 8791 -1012 -766 932 C ATOM 2844 CG1 VAL A1149 248.135 19.297 122.335 1.00 67.60 C ANISOU 2844 CG1 VAL A1149 10456 6760 8468 -941 -616 855 C ATOM 2845 CG2 VAL A1149 246.778 18.334 124.200 1.00 72.79 C ANISOU 2845 CG2 VAL A1149 11320 7360 8979 -1165 -697 1018 C ATOM 2846 N ILE A1150 250.949 16.920 122.930 1.00 75.16 N ANISOU 2846 N ILE A1150 11457 7578 9521 -712 -1142 740 N ATOM 2847 CA ILE A1150 252.236 16.887 122.239 1.00 74.95 C ANISOU 2847 CA ILE A1150 11281 7644 9551 -558 -1208 580 C ATOM 2848 C ILE A1150 252.422 15.565 121.506 1.00 75.77 C ANISOU 2848 C ILE A1150 11381 7666 9741 -399 -1412 496 C ATOM 2849 O ILE A1150 252.865 15.539 120.351 1.00 77.65 O ANISOU 2849 O ILE A1150 11459 8017 10030 -283 -1392 358 O ATOM 2850 CB ILE A1150 253.378 17.151 123.236 1.00 76.10 C ANISOU 2850 CB ILE A1150 11423 7833 9661 -552 -1290 540 C ATOM 2851 CG1 ILE A1150 253.435 18.635 123.598 1.00 75.50 C ANISOU 2851 CG1 ILE A1150 11299 7877 9511 -677 -1078 570 C ATOM 2852 CG2 ILE A1150 254.704 16.677 122.675 1.00 80.42 C ANISOU 2852 CG2 ILE A1150 11823 8471 10260 -370 -1439 348 C ATOM 2853 CD1 ILE A1150 254.464 18.965 124.656 1.00 77.28 C ANISOU 2853 CD1 ILE A1150 11529 8145 9689 -695 -1140 546 C ATOM 2854 N THR A1151 252.089 14.447 122.158 1.00 80.51 N ANISOU 2854 N THR A1151 12165 8074 10349 -403 -1626 574 N ATOM 2855 CA THR A1151 252.197 13.147 121.500 1.00 86.77 C ANISOU 2855 CA THR A1151 12993 8748 11228 -246 -1861 495 C ATOM 2856 C THR A1151 251.304 13.070 120.269 1.00 84.32 C ANISOU 2856 C THR A1151 12620 8461 10957 -238 -1735 495 C ATOM 2857 O THR A1151 251.671 12.436 119.273 1.00 83.89 O ANISOU 2857 O THR A1151 12474 8419 10982 -67 -1840 352 O ATOM 2858 CB THR A1151 251.849 12.027 122.484 1.00 88.04 C ANISOU 2858 CB THR A1151 13419 8664 11367 -307 -2130 620 C ATOM 2859 OG1 THR A1151 252.730 12.091 123.613 1.00 89.68 O ANISOU 2859 OG1 THR A1151 13687 8847 11538 -309 -2263 616 O ATOM 2860 CG2 THR A1151 251.991 10.663 121.824 1.00 89.29 C ANISOU 2860 CG2 THR A1151 13647 8659 11620 -131 -2422 530 C ATOM 2861 N THR A1152 250.136 13.718 120.311 1.00 83.66 N ANISOU 2861 N THR A1152 12574 8398 10816 -410 -1517 634 N ATOM 2862 CA THR A1152 249.268 13.750 119.139 1.00 81.51 C ANISOU 2862 CA THR A1152 12235 8159 10576 -405 -1386 634 C ATOM 2863 C THR A1152 249.942 14.473 117.978 1.00 76.39 C ANISOU 2863 C THR A1152 11362 7698 9966 -304 -1253 483 C ATOM 2864 O THR A1152 249.862 14.027 116.827 1.00 76.09 O ANISOU 2864 O THR A1152 11237 7687 9987 -205 -1269 398 O ATOM 2865 CB THR A1152 247.936 14.412 119.493 1.00 82.85 C ANISOU 2865 CB THR A1152 12468 8343 10668 -595 -1185 782 C ATOM 2866 OG1 THR A1152 247.313 13.691 120.564 1.00 82.61 O ANISOU 2866 OG1 THR A1152 12634 8186 10569 -731 -1309 916 O ATOM 2867 CG2 THR A1152 247.002 14.419 118.289 1.00 82.26 C ANISOU 2867 CG2 THR A1152 12330 8296 10628 -583 -1065 779 C ATOM 2868 N PHE A1153 250.623 15.585 118.262 1.00 76.25 N ANISOU 2868 N PHE A1153 11250 7821 9901 -347 -1130 450 N ATOM 2869 CA PHE A1153 251.369 16.285 117.224 1.00 78.72 C ANISOU 2869 CA PHE A1153 11361 8337 10214 -302 -1023 315 C ATOM 2870 C PHE A1153 252.526 15.455 116.687 1.00 82.95 C ANISOU 2870 C PHE A1153 11761 8958 10798 -119 -1202 114 C ATOM 2871 O PHE A1153 252.959 15.681 115.551 1.00 89.17 O ANISOU 2871 O PHE A1153 12365 9933 11584 -76 -1137 -19 O ATOM 2872 CB PHE A1153 251.902 17.615 117.755 1.00 78.73 C ANISOU 2872 CB PHE A1153 11321 8457 10136 -414 -888 332 C ATOM 2873 CG PHE A1153 250.856 18.681 117.887 1.00 75.74 C ANISOU 2873 CG PHE A1153 11018 8049 9712 -560 -699 464 C ATOM 2874 CD1 PHE A1153 250.080 19.047 116.801 1.00 74.90 C ANISOU 2874 CD1 PHE A1153 10875 7967 9618 -587 -581 480 C ATOM 2875 CD2 PHE A1153 250.664 19.334 119.092 1.00 74.17 C ANISOU 2875 CD2 PHE A1153 10921 7804 9456 -659 -655 553 C ATOM 2876 CE1 PHE A1153 249.118 20.034 116.920 1.00 74.34 C ANISOU 2876 CE1 PHE A1153 10874 7860 9510 -689 -441 573 C ATOM 2877 CE2 PHE A1153 249.707 20.324 119.217 1.00 74.38 C ANISOU 2877 CE2 PHE A1153 11004 7814 9444 -760 -507 634 C ATOM 2878 CZ PHE A1153 248.934 20.675 118.129 1.00 75.35 C ANISOU 2878 CZ PHE A1153 11095 7948 9587 -766 -410 638 C ATOM 2879 N ARG A1154 253.036 14.505 117.473 1.00 83.32 N ANISOU 2879 N ARG A1154 11893 8886 10880 -11 -1441 75 N ATOM 2880 CA ARG A1154 254.163 13.690 117.035 1.00 87.07 C ANISOU 2880 CA ARG A1154 12233 9442 11406 204 -1651 -157 C ATOM 2881 C ARG A1154 253.727 12.610 116.053 1.00 85.90 C ANISOU 2881 C ARG A1154 12080 9215 11342 343 -1777 -236 C ATOM 2882 O ARG A1154 254.308 12.471 114.972 1.00 88.22 O ANISOU 2882 O ARG A1154 12162 9703 11656 468 -1783 -441 O ATOM 2883 CB ARG A1154 254.850 13.055 118.245 1.00 93.52 C ANISOU 2883 CB ARG A1154 13169 10127 12237 287 -1904 -177 C ATOM 2884 CG ARG A1154 255.484 14.045 119.202 1.00102.68 C ANISOU 2884 CG ARG A1154 14309 11389 13317 178 -1805 -138 C ATOM 2885 CD ARG A1154 256.224 13.328 120.322 1.00107.86 C ANISOU 2885 CD ARG A1154 15076 11916 13990 279 -2083 -176 C ATOM 2886 NE ARG A1154 257.150 12.320 119.813 1.00112.89 N ANISOU 2886 NE ARG A1154 15603 12587 14702 547 -2355 -431 N ATOM 2887 CZ ARG A1154 258.335 12.594 119.278 1.00116.72 C ANISOU 2887 CZ ARG A1154 15817 13361 15172 675 -2352 -686 C ATOM 2888 NH1 ARG A1154 258.751 13.851 119.182 1.00115.82 N ANISOU 2888 NH1 ARG A1154 15539 13507 14962 527 -2093 -690 N ATOM 2889 NH2 ARG A1154 259.109 11.610 118.840 1.00119.42 N ANISOU 2889 NH2 ARG A1154 16051 13741 15583 945 -2623 -950 N ATOM 2890 N THR A1155 252.703 11.837 116.412 1.00 82.84 N ANISOU 2890 N THR A1155 11922 8564 10990 307 -1881 -79 N ATOM 2891 CA THR A1155 252.338 10.643 115.663 1.00 87.06 C ANISOU 2891 CA THR A1155 12501 8971 11608 446 -2066 -147 C ATOM 2892 C THR A1155 251.202 10.857 114.671 1.00 83.22 C ANISOU 2892 C THR A1155 11990 8505 11124 355 -1865 -61 C ATOM 2893 O THR A1155 251.012 10.016 113.785 1.00 85.00 O ANISOU 2893 O THR A1155 12192 8688 11417 480 -1978 -156 O ATOM 2894 CB THR A1155 251.942 9.520 116.629 1.00 93.31 C ANISOU 2894 CB THR A1155 13586 9443 12424 445 -2357 -27 C ATOM 2895 OG1 THR A1155 250.736 9.880 117.314 1.00 97.79 O ANISOU 2895 OG1 THR A1155 14334 9904 12916 190 -2208 239 O ATOM 2896 CG2 THR A1155 253.042 9.288 117.650 1.00 93.94 C ANISOU 2896 CG2 THR A1155 13714 9477 12503 538 -2583 -103 C ATOM 2897 N GLY A1156 250.446 11.945 114.793 1.00 79.09 N ANISOU 2897 N GLY A1156 11475 8043 10533 155 -1590 100 N ATOM 2898 CA GLY A1156 249.271 12.106 113.962 1.00 76.33 C ANISOU 2898 CA GLY A1156 11130 7687 10187 72 -1426 190 C ATOM 2899 C GLY A1156 248.136 11.165 114.290 1.00 73.64 C ANISOU 2899 C GLY A1156 11006 7115 9860 12 -1538 336 C ATOM 2900 O GLY A1156 247.155 11.112 113.542 1.00 72.63 O ANISOU 2900 O GLY A1156 10877 6978 9740 -36 -1433 392 O ATOM 2901 N THR A1157 248.247 10.409 115.378 1.00 75.74 N ANISOU 2901 N THR A1157 11464 7198 10115 -4 -1761 404 N ATOM 2902 CA THR A1157 247.199 9.521 115.852 1.00 74.81 C ANISOU 2902 CA THR A1157 11584 6869 9971 -124 -1889 567 C ATOM 2903 C THR A1157 246.831 9.903 117.279 1.00 81.07 C ANISOU 2903 C THR A1157 12527 7621 10654 -334 -1854 741 C ATOM 2904 O THR A1157 247.598 10.564 117.984 1.00 81.99 O ANISOU 2904 O THR A1157 12598 7811 10743 -333 -1818 715 O ATOM 2905 CB THR A1157 247.643 8.052 115.803 1.00 71.44 C ANISOU 2905 CB THR A1157 11298 6230 9618 28 -2264 492 C ATOM 2906 OG1 THR A1157 248.660 7.825 116.787 1.00 72.31 O ANISOU 2906 OG1 THR A1157 11484 6265 9725 93 -2479 448 O ATOM 2907 CG2 THR A1157 248.193 7.703 114.429 1.00 73.32 C ANISOU 2907 CG2 THR A1157 11347 6551 9962 269 -2312 266 C ATOM 2908 N TRP A1158 245.640 9.481 117.704 1.00 83.92 N ANISOU 2908 N TRP A1158 13060 7889 10938 -530 -1862 911 N ATOM 2909 CA TRP A1158 245.169 9.755 119.054 1.00 85.13 C ANISOU 2909 CA TRP A1158 13349 8038 10958 -763 -1830 1069 C ATOM 2910 C TRP A1158 245.506 8.635 120.033 1.00 87.69 C ANISOU 2910 C TRP A1158 13929 8146 11244 -827 -2171 1150 C ATOM 2911 O TRP A1158 244.803 8.474 121.038 1.00 93.21 O ANISOU 2911 O TRP A1158 14793 8817 11804 -1082 -2195 1315 O ATOM 2912 CB TRP A1158 243.659 10.023 119.048 1.00 84.37 C ANISOU 2912 CB TRP A1158 13270 8027 10761 -977 -1634 1193 C ATOM 2913 CG TRP A1158 242.787 8.858 118.638 1.00 87.26 C ANISOU 2913 CG TRP A1158 13782 8262 11109 -1060 -1780 1273 C ATOM 2914 CD1 TRP A1158 243.177 7.567 118.417 1.00 91.05 C ANISOU 2914 CD1 TRP A1158 14426 8518 11651 -980 -2100 1265 C ATOM 2915 CD2 TRP A1158 241.372 8.891 118.405 1.00 87.59 C ANISOU 2915 CD2 TRP A1158 13825 8394 11062 -1241 -1626 1361 C ATOM 2916 NE1 TRP A1158 242.095 6.798 118.065 1.00 92.19 N ANISOU 2916 NE1 TRP A1158 14690 8593 11746 -1119 -2154 1362 N ATOM 2917 CE2 TRP A1158 240.976 7.587 118.048 1.00 90.59 C ANISOU 2917 CE2 TRP A1158 14379 8597 11446 -1287 -1855 1422 C ATOM 2918 CE3 TRP A1158 240.403 9.898 118.464 1.00 87.91 C ANISOU 2918 CE3 TRP A1158 13735 8651 11018 -1358 -1334 1378 C ATOM 2919 CZ2 TRP A1158 239.654 7.263 117.750 1.00 90.42 C ANISOU 2919 CZ2 TRP A1158 14394 8626 11335 -1470 -1780 1512 C ATOM 2920 CZ3 TRP A1158 239.091 9.574 118.167 1.00 89.14 C ANISOU 2920 CZ3 TRP A1158 13909 8869 11090 -1515 -1264 1445 C ATOM 2921 CH2 TRP A1158 238.729 8.267 117.815 1.00 89.49 C ANISOU 2921 CH2 TRP A1158 14121 8753 11130 -1582 -1476 1518 C ATOM 2922 N ASP A1159 246.564 7.864 119.761 1.00 86.61 N ANISOU 2922 N ASP A1159 13826 7865 11216 -605 -2450 1026 N ATOM 2923 CA ASP A1159 246.880 6.702 120.587 1.00 85.46 C ANISOU 2923 CA ASP A1159 13960 7463 11048 -642 -2838 1095 C ATOM 2924 C ASP A1159 247.085 7.079 122.049 1.00 86.77 C ANISOU 2924 C ASP A1159 14239 7637 11093 -828 -2854 1215 C ATOM 2925 O ASP A1159 246.872 6.247 122.938 1.00 93.36 O ANISOU 2925 O ASP A1159 15354 8282 11838 -1002 -3119 1360 O ATOM 2926 CB ASP A1159 248.120 5.994 120.043 1.00 87.27 C ANISOU 2926 CB ASP A1159 14159 7572 11427 -313 -3133 880 C ATOM 2927 CG ASP A1159 247.856 5.282 118.733 1.00 87.74 C ANISOU 2927 CG ASP A1159 14177 7571 11590 -150 -3214 772 C ATOM 2928 OD1 ASP A1159 246.691 4.909 118.485 1.00 87.88 O ANISOU 2928 OD1 ASP A1159 14309 7525 11555 -325 -3174 914 O ATOM 2929 OD2 ASP A1159 248.813 5.097 117.952 1.00 88.23 O ANISOU 2929 OD2 ASP A1159 14076 7672 11776 148 -3316 531 O ATOM 2930 N ALA A1160 247.489 8.322 122.319 1.00 82.80 N ANISOU 2930 N ALA A1160 13538 7347 10575 -812 -2587 1163 N ATOM 2931 CA ALA A1160 247.619 8.781 123.696 1.00 80.92 C ANISOU 2931 CA ALA A1160 13386 7145 10216 -995 -2567 1271 C ATOM 2932 C ALA A1160 246.280 8.861 124.418 1.00 82.91 C ANISOU 2932 C ALA A1160 13758 7454 10289 -1339 -2447 1470 C ATOM 2933 O ALA A1160 246.267 8.974 125.648 1.00 85.34 O ANISOU 2933 O ALA A1160 14184 7774 10467 -1539 -2487 1580 O ATOM 2934 CB ALA A1160 248.309 10.145 123.732 1.00 80.78 C ANISOU 2934 CB ALA A1160 13124 7345 10222 -900 -2303 1161 C ATOM 2935 N TYR A1161 245.164 8.807 123.692 1.00 82.91 N ANISOU 2935 N TYR A1161 13718 7518 10268 -1420 -2300 1507 N ATOM 2936 CA TYR A1161 243.834 8.821 124.285 1.00 83.86 C ANISOU 2936 CA TYR A1161 13919 7741 10202 -1748 -2187 1664 C ATOM 2937 C TYR A1161 243.142 7.467 124.191 1.00 87.11 C ANISOU 2937 C TYR A1161 14577 7971 10549 -1914 -2442 1793 C ATOM 2938 O TYR A1161 241.933 7.381 124.435 1.00 90.93 O ANISOU 2938 O TYR A1161 15105 8572 10872 -2194 -2341 1908 O ATOM 2939 CB TYR A1161 242.967 9.893 123.618 1.00 81.75 C ANISOU 2939 CB TYR A1161 13411 7720 9932 -1740 -1815 1602 C ATOM 2940 CG TYR A1161 243.511 11.298 123.740 1.00 79.21 C ANISOU 2940 CG TYR A1161 12880 7566 9651 -1619 -1575 1493 C ATOM 2941 CD1 TYR A1161 243.226 12.079 124.852 1.00 76.34 C ANISOU 2941 CD1 TYR A1161 12496 7363 9149 -1793 -1439 1534 C ATOM 2942 CD2 TYR A1161 244.301 11.847 122.738 1.00 79.05 C ANISOU 2942 CD2 TYR A1161 12686 7558 9793 -1348 -1494 1346 C ATOM 2943 CE1 TYR A1161 243.719 13.364 124.968 1.00 75.04 C ANISOU 2943 CE1 TYR A1161 12164 7326 9020 -1683 -1246 1435 C ATOM 2944 CE2 TYR A1161 244.799 13.133 122.844 1.00 77.38 C ANISOU 2944 CE2 TYR A1161 12314 7488 9601 -1271 -1299 1262 C ATOM 2945 CZ TYR A1161 244.504 13.887 123.961 1.00 74.53 C ANISOU 2945 CZ TYR A1161 11956 7247 9116 -1431 -1183 1309 C ATOM 2946 OH TYR A1161 244.998 15.168 124.072 1.00 74.22 O ANISOU 2946 OH TYR A1161 11780 7324 9097 -1355 -1013 1226 O ATOM 2947 N GLY A1162 243.870 6.414 123.838 1.00 88.65 N ANISOU 2947 N GLY A1162 14931 7894 10857 -1751 -2783 1763 N ATOM 2948 CA GLY A1162 243.273 5.105 123.678 1.00 88.23 C ANISOU 2948 CA GLY A1162 15141 7627 10754 -1894 -3068 1881 C ATOM 2949 C GLY A1162 242.669 4.901 122.303 1.00 87.95 C ANISOU 2949 C GLY A1162 14993 7607 10816 -1771 -2966 1809 C ATOM 2950 O GLY A1162 242.796 5.723 121.389 1.00 84.94 O ANISOU 2950 O GLY A1162 14333 7386 10554 -1552 -2698 1660 O ATOM 2951 N SER A1163 241.984 3.763 122.164 1.00 90.38 N ANISOU 2951 N SER A1163 15542 7738 11059 -1939 -3203 1930 N ATOM 2952 CA SER A1163 241.374 3.420 120.884 1.00 92.89 C ANISOU 2952 CA SER A1163 15786 8045 11461 -1840 -3145 1874 C ATOM 2953 C SER A1163 240.152 4.281 120.589 1.00 94.84 C ANISOU 2953 C SER A1163 15822 8604 11609 -2005 -2734 1904 C ATOM 2954 O SER A1163 239.865 4.566 119.420 1.00 97.30 O ANISOU 2954 O SER A1163 15942 8996 12031 -1832 -2555 1797 O ATOM 2955 CB SER A1163 241.000 1.938 120.859 1.00 91.83 C ANISOU 2955 CB SER A1163 15997 7616 11277 -1987 -3543 1999 C ATOM 2956 OG SER A1163 240.045 1.634 121.861 1.00 92.98 O ANISOU 2956 OG SER A1163 16262 7908 11157 -2402 -3535 2167 O ATOM 2957 N GLY A1164 239.425 4.700 121.616 1.00 96.14 N ANISOU 2957 N GLY A1164 16009 8956 11562 -2331 -2594 2030 N ATOM 2958 CA GLY A1164 238.249 5.527 121.433 1.00 99.98 C ANISOU 2958 CA GLY A1164 16286 9760 11943 -2474 -2230 2026 C ATOM 2959 C GLY A1164 236.963 4.726 121.472 1.00104.38 C ANISOU 2959 C GLY A1164 16988 10359 12313 -2814 -2287 2170 C ATOM 2960 O GLY A1164 236.936 3.524 121.756 1.00112.32 O ANISOU 2960 O GLY A1164 18296 11137 13245 -2995 -2620 2308 O ATOM 2961 N SER A1165 235.867 5.425 121.179 1.00104.15 N ANISOU 2961 N SER A1165 16743 10631 12197 -2908 -1969 2131 N ATOM 2962 CA SER A1165 234.550 4.803 121.157 1.00102.14 C ANISOU 2962 CA SER A1165 16566 10496 11745 -3240 -1967 2241 C ATOM 2963 C SER A1165 234.289 4.208 119.781 1.00101.74 C ANISOU 2963 C SER A1165 16516 10300 11841 -3072 -2018 2204 C ATOM 2964 O SER A1165 234.191 4.962 118.803 1.00 98.91 O ANISOU 2964 O SER A1165 15904 10046 11630 -2809 -1778 2057 O ATOM 2965 CB SER A1165 233.467 5.813 121.497 1.00104.30 C ANISOU 2965 CB SER A1165 16587 11194 11850 -3404 -1616 2182 C ATOM 2966 OG SER A1165 232.185 5.209 121.476 1.00104.85 O ANISOU 2966 OG SER A1165 16704 11428 11707 -3740 -1607 2270 O ATOM 2967 N PRO A 297 234.168 2.885 119.653 1.00105.21 N ANISOU 2967 N PRO A 297 17243 10492 12241 -3220 -2338 2331 N ATOM 2968 CA PRO A 297 233.922 2.305 118.324 1.00106.91 C ANISOU 2968 CA PRO A 297 17456 10568 12598 -3051 -2392 2283 C ATOM 2969 C PRO A 297 232.569 2.677 117.742 1.00109.08 C ANISOU 2969 C PRO A 297 17533 11139 12774 -3180 -2101 2262 C ATOM 2970 O PRO A 297 232.433 2.724 116.513 1.00104.60 O ANISOU 2970 O PRO A 297 16835 10542 12366 -2945 -2012 2162 O ATOM 2971 CB PRO A 297 234.036 0.794 118.573 1.00109.94 C ANISOU 2971 CB PRO A 297 18133 10723 12918 -3167 -2801 2363 C ATOM 2972 CG PRO A 297 233.731 0.627 120.029 1.00112.94 C ANISOU 2972 CG PRO A 297 18623 11261 13028 -3532 -2870 2475 C ATOM 2973 CD PRO A 297 234.274 1.856 120.702 1.00108.78 C ANISOU 2973 CD PRO A 297 17964 10846 12519 -3481 -2659 2454 C ATOM 2974 N GLY A 298 231.567 2.949 118.581 1.00114.44 N ANISOU 2974 N GLY A 298 18170 12124 13187 -3545 -1952 2337 N ATOM 2975 CA GLY A 298 230.253 3.295 118.062 1.00115.59 C ANISOU 2975 CA GLY A 298 18109 12582 13226 -3661 -1688 2289 C ATOM 2976 C GLY A 298 230.240 4.618 117.318 1.00107.60 C ANISOU 2976 C GLY A 298 16746 11752 12383 -3315 -1352 2084 C ATOM 2977 O GLY A 298 229.647 4.729 116.241 1.00103.98 O ANISOU 2977 O GLY A 298 16149 11355 12003 -3191 -1222 2009 O ATOM 2978 N ARG A 299 230.892 5.639 117.879 1.00104.07 N ANISOU 2978 N ARG A 299 16170 11384 11988 -3166 -1226 1997 N ATOM 2979 CA ARG A 299 230.944 6.937 117.217 1.00 98.95 C ANISOU 2979 CA ARG A 299 15229 10875 11492 -2853 -948 1815 C ATOM 2980 C ARG A 299 231.917 6.946 116.048 1.00 93.47 C ANISOU 2980 C ARG A 299 14515 9918 11080 -2478 -1003 1740 C ATOM 2981 O ARG A 299 231.688 7.658 115.064 1.00 93.43 O ANISOU 2981 O ARG A 299 14313 9994 11195 -2264 -816 1621 O ATOM 2982 CB ARG A 299 231.328 8.031 118.217 1.00 98.31 C ANISOU 2982 CB ARG A 299 15034 10955 11364 -2832 -814 1747 C ATOM 2983 CG ARG A 299 230.273 8.319 119.271 1.00100.44 C ANISOU 2983 CG ARG A 299 15227 11584 11352 -3160 -689 1750 C ATOM 2984 CD ARG A 299 230.712 9.437 120.207 1.00103.95 C ANISOU 2984 CD ARG A 299 15552 12175 11769 -3101 -566 1660 C ATOM 2985 NE ARG A 299 229.673 9.772 121.178 1.00104.43 N ANISOU 2985 NE ARG A 299 15496 12629 11552 -3394 -433 1618 N ATOM 2986 CZ ARG A 299 228.756 10.719 120.997 1.00104.46 C ANISOU 2986 CZ ARG A 299 15233 12952 11506 -3325 -199 1436 C ATOM 2987 NH1 ARG A 299 228.746 11.433 119.879 1.00101.12 N ANISOU 2987 NH1 ARG A 299 14663 12464 11293 -2987 -83 1306 N ATOM 2988 NH2 ARG A 299 227.849 10.953 121.935 1.00109.10 N ANISOU 2988 NH2 ARG A 299 15698 13933 11822 -3598 -96 1371 N ATOM 2989 N VAL A 300 233.000 6.170 116.129 1.00 89.58 N ANISOU 2989 N VAL A 300 14220 9130 10688 -2396 -1269 1795 N ATOM 2990 CA VAL A 300 234.001 6.198 115.069 1.00 83.12 C ANISOU 2990 CA VAL A 300 13348 8119 10117 -2041 -1321 1689 C ATOM 2991 C VAL A 300 233.539 5.437 113.832 1.00 80.52 C ANISOU 2991 C VAL A 300 13036 7691 9865 -1974 -1381 1679 C ATOM 2992 O VAL A 300 234.039 5.699 112.730 1.00 81.14 O ANISOU 2992 O VAL A 300 12985 7719 10124 -1694 -1328 1559 O ATOM 2993 CB VAL A 300 235.346 5.646 115.575 1.00 80.34 C ANISOU 2993 CB VAL A 300 13169 7513 9845 -1941 -1597 1705 C ATOM 2994 CG1 VAL A 300 235.370 4.125 115.521 1.00 81.49 C ANISOU 2994 CG1 VAL A 300 13598 7388 9976 -2038 -1949 1806 C ATOM 2995 CG2 VAL A 300 236.503 6.242 114.788 1.00 75.57 C ANISOU 2995 CG2 VAL A 300 12402 6858 9455 -1579 -1548 1542 C ATOM 2996 N GLN A 301 232.588 4.510 113.974 1.00 80.49 N ANISOU 2996 N GLN A 301 13188 7677 9715 -2245 -1489 1801 N ATOM 2997 CA GLN A 301 232.076 3.806 112.805 1.00 79.63 C ANISOU 2997 CA GLN A 301 13098 7485 9673 -2194 -1540 1792 C ATOM 2998 C GLN A 301 231.122 4.680 112.003 1.00 80.71 C ANISOU 2998 C GLN A 301 12971 7882 9812 -2142 -1220 1705 C ATOM 2999 O GLN A 301 231.123 4.630 110.767 1.00 79.74 O ANISOU 2999 O GLN A 301 12757 7707 9832 -1940 -1179 1625 O ATOM 3000 CB GLN A 301 231.391 2.506 113.225 1.00 79.13 C ANISOU 3000 CB GLN A 301 13313 7312 9440 -2526 -1786 1962 C ATOM 3001 CG GLN A 301 232.355 1.404 113.637 1.00 77.60 C ANISOU 3001 CG GLN A 301 13429 6762 9293 -2515 -2192 2035 C ATOM 3002 CD GLN A 301 233.389 1.101 112.568 1.00 75.38 C ANISOU 3002 CD GLN A 301 13121 6245 9275 -2114 -2333 1888 C ATOM 3003 OE1 GLN A 301 234.488 1.656 112.575 1.00 72.80 O ANISOU 3003 OE1 GLN A 301 12685 5890 9088 -1849 -2313 1767 O ATOM 3004 NE2 GLN A 301 233.040 0.216 111.641 1.00 75.40 N ANISOU 3004 NE2 GLN A 301 13212 6102 9333 -2078 -2476 1885 N ATOM 3005 N ALA A 302 230.303 5.488 112.684 1.00 83.09 N ANISOU 3005 N ALA A 302 13145 8472 9954 -2313 -1004 1703 N ATOM 3006 CA ALA A 302 229.444 6.428 111.972 1.00 82.36 C ANISOU 3006 CA ALA A 302 12799 8621 9874 -2223 -724 1591 C ATOM 3007 C ALA A 302 230.266 7.432 111.177 1.00 80.98 C ANISOU 3007 C ALA A 302 12458 8400 9912 -1873 -604 1456 C ATOM 3008 O ALA A 302 229.788 7.969 110.171 1.00 83.21 O ANISOU 3008 O ALA A 302 12580 8768 10267 -1736 -450 1369 O ATOM 3009 CB ALA A 302 228.517 7.147 112.952 1.00 81.11 C ANISOU 3009 CB ALA A 302 12522 8792 9504 -2439 -546 1572 C ATOM 3010 N LEU A 303 231.500 7.699 111.611 1.00 79.21 N ANISOU 3010 N LEU A 303 12273 8049 9774 -1745 -681 1438 N ATOM 3011 CA LEU A 303 232.406 8.505 110.802 1.00 77.27 C ANISOU 3011 CA LEU A 303 11893 7755 9712 -1450 -603 1321 C ATOM 3012 C LEU A 303 232.753 7.786 109.505 1.00 75.22 C ANISOU 3012 C LEU A 303 11644 7338 9597 -1287 -703 1284 C ATOM 3013 O LEU A 303 232.684 8.370 108.417 1.00 74.56 O ANISOU 3013 O LEU A 303 11409 7312 9608 -1129 -570 1197 O ATOM 3014 CB LEU A 303 233.674 8.829 111.593 1.00 75.12 C ANISOU 3014 CB LEU A 303 11663 7399 9480 -1376 -681 1308 C ATOM 3015 CG LEU A 303 234.799 9.533 110.827 1.00 71.19 C ANISOU 3015 CG LEU A 303 11043 6858 9146 -1111 -636 1192 C ATOM 3016 CD1 LEU A 303 234.327 10.882 110.311 1.00 66.63 C ANISOU 3016 CD1 LEU A 303 10284 6449 8583 -1038 -395 1116 C ATOM 3017 CD2 LEU A 303 236.032 9.689 111.702 1.00 69.58 C ANISOU 3017 CD2 LEU A 303 10894 6582 8961 -1065 -738 1184 C ATOM 3018 N ARG A 304 233.118 6.506 109.602 1.00 75.29 N ANISOU 3018 N ARG A 304 11841 7146 9618 -1327 -958 1344 N ATOM 3019 CA ARG A 304 233.502 5.759 108.410 1.00 73.02 C ANISOU 3019 CA ARG A 304 11564 6712 9469 -1152 -1082 1281 C ATOM 3020 C ARG A 304 232.325 5.574 107.462 1.00 73.94 C ANISOU 3020 C ARG A 304 11619 6909 9567 -1204 -974 1291 C ATOM 3021 O ARG A 304 232.519 5.510 106.243 1.00 75.09 O ANISOU 3021 O ARG A 304 11670 7029 9834 -1026 -953 1201 O ATOM 3022 CB ARG A 304 234.096 4.406 108.804 1.00 71.07 C ANISOU 3022 CB ARG A 304 11560 6209 9236 -1174 -1425 1330 C ATOM 3023 CG ARG A 304 235.624 4.384 108.868 1.00 70.05 C ANISOU 3023 CG ARG A 304 11424 5957 9234 -939 -1578 1217 C ATOM 3024 CD ARG A 304 236.190 5.658 109.483 1.00 69.04 C ANISOU 3024 CD ARG A 304 11155 5981 9095 -902 -1391 1180 C ATOM 3025 NE ARG A 304 237.647 5.630 109.576 1.00 68.36 N ANISOU 3025 NE ARG A 304 11050 5811 9112 -696 -1535 1066 N ATOM 3026 CZ ARG A 304 238.319 5.444 110.708 1.00 67.84 C ANISOU 3026 CZ ARG A 304 11114 5651 9010 -736 -1696 1105 C ATOM 3027 NH1 ARG A 304 239.645 5.433 110.702 1.00 67.17 N ANISOU 3027 NH1 ARG A 304 10983 5516 9021 -528 -1823 973 N ATOM 3028 NH2 ARG A 304 237.664 5.269 111.847 1.00 68.94 N ANISOU 3028 NH2 ARG A 304 11420 5771 9004 -995 -1731 1266 N ATOM 3029 N HIS A 305 231.105 5.493 107.996 1.00 74.04 N ANISOU 3029 N HIS A 305 11671 7046 9416 -1456 -903 1388 N ATOM 3030 CA HIS A 305 229.927 5.392 107.141 1.00 74.11 C ANISOU 3030 CA HIS A 305 11601 7166 9393 -1512 -785 1387 C ATOM 3031 C HIS A 305 229.784 6.626 106.261 1.00 76.37 C ANISOU 3031 C HIS A 305 11647 7605 9767 -1323 -539 1268 C ATOM 3032 O HIS A 305 229.643 6.519 105.037 1.00 77.55 O ANISOU 3032 O HIS A 305 11720 7733 10012 -1196 -505 1213 O ATOM 3033 CB HIS A 305 228.672 5.201 107.994 1.00 72.67 C ANISOU 3033 CB HIS A 305 11468 7155 8987 -1835 -737 1487 C ATOM 3034 CG HIS A 305 228.423 3.782 108.398 1.00 71.77 C ANISOU 3034 CG HIS A 305 11612 6891 8766 -2077 -992 1626 C ATOM 3035 ND1 HIS A 305 227.250 3.376 108.997 1.00 73.23 N ANISOU 3035 ND1 HIS A 305 11860 7241 8723 -2420 -979 1728 N ATOM 3036 CD2 HIS A 305 229.193 2.674 108.290 1.00 73.17 C ANISOU 3036 CD2 HIS A 305 12010 6769 9022 -2033 -1289 1673 C ATOM 3037 CE1 HIS A 305 227.308 2.080 109.241 1.00 75.08 C ANISOU 3037 CE1 HIS A 305 12369 7265 8893 -2607 -1262 1859 C ATOM 3038 NE2 HIS A 305 228.477 1.629 108.822 1.00 75.10 N ANISOU 3038 NE2 HIS A 305 12480 6966 9090 -2359 -1467 1824 N ATOM 3039 N GLY A 306 229.829 7.813 106.871 1.00 76.89 N ANISOU 3039 N GLY A 306 11604 7815 9797 -1307 -384 1227 N ATOM 3040 CA GLY A 306 229.587 9.037 106.128 1.00 77.97 C ANISOU 3040 CA GLY A 306 11550 8079 9995 -1156 -185 1127 C ATOM 3041 C GLY A 306 230.635 9.330 105.076 1.00 80.43 C ANISOU 3041 C GLY A 306 11801 8288 10473 -929 -196 1052 C ATOM 3042 O GLY A 306 230.334 9.962 104.059 1.00 83.38 O ANISOU 3042 O GLY A 306 12055 8724 10903 -827 -81 991 O ATOM 3043 N VAL A 307 231.872 8.883 105.297 1.00 80.41 N ANISOU 3043 N VAL A 307 11872 8145 10537 -857 -342 1046 N ATOM 3044 CA VAL A 307 232.926 9.124 104.317 1.00 78.25 C ANISOU 3044 CA VAL A 307 11510 7828 10392 -661 -353 950 C ATOM 3045 C VAL A 307 232.649 8.347 103.037 1.00 80.75 C ANISOU 3045 C VAL A 307 11802 8102 10776 -596 -397 916 C ATOM 3046 O VAL A 307 232.707 8.899 101.931 1.00 82.16 O ANISOU 3046 O VAL A 307 11852 8351 11013 -497 -295 847 O ATOM 3047 CB VAL A 307 234.302 8.770 104.906 1.00 73.87 C ANISOU 3047 CB VAL A 307 11019 7168 9881 -591 -514 920 C ATOM 3048 CG1 VAL A 307 235.383 8.934 103.847 1.00 71.38 C ANISOU 3048 CG1 VAL A 307 10580 6868 9673 -406 -527 791 C ATOM 3049 CG2 VAL A 307 234.597 9.641 106.114 1.00 73.78 C ANISOU 3049 CG2 VAL A 307 11019 7210 9805 -653 -453 950 C ATOM 3050 N LEU A 308 232.336 7.055 103.167 1.00 81.53 N ANISOU 3050 N LEU A 308 12039 8081 10858 -665 -564 969 N ATOM 3051 CA LEU A 308 232.029 6.251 101.988 1.00 80.92 C ANISOU 3051 CA LEU A 308 11951 7951 10842 -604 -622 934 C ATOM 3052 C LEU A 308 230.788 6.762 101.271 1.00 83.19 C ANISOU 3052 C LEU A 308 12139 8377 11094 -660 -431 952 C ATOM 3053 O LEU A 308 230.673 6.613 100.048 1.00 88.86 O ANISOU 3053 O LEU A 308 12777 9108 11880 -568 -403 894 O ATOM 3054 CB LEU A 308 231.858 4.780 102.376 1.00 77.61 C ANISOU 3054 CB LEU A 308 11740 7350 10397 -694 -869 1001 C ATOM 3055 CG LEU A 308 233.120 3.916 102.481 1.00 78.48 C ANISOU 3055 CG LEU A 308 11948 7273 10596 -550 -1138 926 C ATOM 3056 CD1 LEU A 308 234.056 4.389 103.587 1.00 77.22 C ANISOU 3056 CD1 LEU A 308 11816 7102 10423 -535 -1178 924 C ATOM 3057 CD2 LEU A 308 232.747 2.455 102.682 1.00 79.88 C ANISOU 3057 CD2 LEU A 308 12365 7240 10748 -645 -1413 1000 C ATOM 3058 N VAL A 309 229.854 7.371 102.004 1.00 79.40 N ANISOU 3058 N VAL A 309 11650 8016 10503 -801 -305 1015 N ATOM 3059 CA VAL A 309 228.686 7.964 101.363 1.00 78.50 C ANISOU 3059 CA VAL A 309 11423 8049 10356 -824 -135 1001 C ATOM 3060 C VAL A 309 229.090 9.185 100.548 1.00 77.81 C ANISOU 3060 C VAL A 309 11191 8024 10347 -667 -7 917 C ATOM 3061 O VAL A 309 228.590 9.401 99.436 1.00 78.79 O ANISOU 3061 O VAL A 309 11233 8196 10509 -612 67 882 O ATOM 3062 CB VAL A 309 227.617 8.309 102.415 1.00 80.71 C ANISOU 3062 CB VAL A 309 11706 8478 10484 -1001 -50 1048 C ATOM 3063 CG1 VAL A 309 226.502 9.128 101.789 1.00 78.66 C ANISOU 3063 CG1 VAL A 309 11301 8388 10199 -975 118 990 C ATOM 3064 CG2 VAL A 309 227.063 7.038 103.037 1.00 84.48 C ANISOU 3064 CG2 VAL A 309 12333 8917 10848 -1218 -179 1149 C ATOM 3065 N LEU A 310 230.003 10.001 101.081 1.00 75.87 N ANISOU 3065 N LEU A 310 10929 7778 10120 -612 9 890 N ATOM 3066 CA LEU A 310 230.507 11.138 100.318 1.00 71.14 C ANISOU 3066 CA LEU A 310 10228 7225 9579 -501 97 825 C ATOM 3067 C LEU A 310 231.284 10.672 99.094 1.00 68.15 C ANISOU 3067 C LEU A 310 9798 6810 9286 -405 45 768 C ATOM 3068 O LEU A 310 231.233 11.309 98.036 1.00 70.10 O ANISOU 3068 O LEU A 310 9959 7117 9560 -359 120 730 O ATOM 3069 CB LEU A 310 231.381 12.024 101.206 1.00 71.60 C ANISOU 3069 CB LEU A 310 10295 7287 9623 -488 105 814 C ATOM 3070 CG LEU A 310 230.682 12.733 102.365 1.00 70.23 C ANISOU 3070 CG LEU A 310 10142 7181 9361 -563 169 836 C ATOM 3071 CD1 LEU A 310 231.701 13.417 103.261 1.00 69.94 C ANISOU 3071 CD1 LEU A 310 10131 7126 9319 -550 152 828 C ATOM 3072 CD2 LEU A 310 229.661 13.734 101.847 1.00 69.19 C ANISOU 3072 CD2 LEU A 310 9937 7140 9212 -531 277 795 C ATOM 3073 N ARG A 311 232.009 9.558 99.218 1.00 65.66 N ANISOU 3073 N ARG A 311 9536 6404 9008 -373 -101 749 N ATOM 3074 CA ARG A 311 232.694 8.994 98.061 1.00 71.33 C ANISOU 3074 CA ARG A 311 10182 7118 9801 -266 -165 656 C ATOM 3075 C ARG A 311 231.698 8.458 97.042 1.00 72.79 C ANISOU 3075 C ARG A 311 10348 7309 10000 -275 -139 664 C ATOM 3076 O ARG A 311 231.881 8.639 95.832 1.00 76.11 O ANISOU 3076 O ARG A 311 10660 7801 10457 -214 -93 595 O ATOM 3077 CB ARG A 311 233.653 7.888 98.501 1.00 77.40 C ANISOU 3077 CB ARG A 311 11021 7776 10611 -198 -368 603 C ATOM 3078 CG ARG A 311 234.840 8.375 99.311 1.00 83.02 C ANISOU 3078 CG ARG A 311 11723 8501 11321 -161 -405 563 C ATOM 3079 CD ARG A 311 235.668 7.210 99.828 1.00 86.05 C ANISOU 3079 CD ARG A 311 12196 8752 11746 -80 -642 506 C ATOM 3080 NE ARG A 311 236.841 7.663 100.569 1.00 89.21 N ANISOU 3080 NE ARG A 311 12571 9179 12143 -33 -680 453 N ATOM 3081 CZ ARG A 311 237.670 6.856 101.222 1.00 94.61 C ANISOU 3081 CZ ARG A 311 13337 9751 12859 46 -896 397 C ATOM 3082 NH1 ARG A 311 237.454 5.547 101.230 1.00 97.63 N ANISOU 3082 NH1 ARG A 311 13854 9962 13277 84 -1113 394 N ATOM 3083 NH2 ARG A 311 238.714 7.357 101.868 1.00 97.54 N ANISOU 3083 NH2 ARG A 311 13669 10171 13222 86 -914 344 N ATOM 3084 N ALA A 312 230.639 7.795 97.513 1.00 73.27 N ANISOU 3084 N ALA A 312 10510 7314 10015 -374 -168 749 N ATOM 3085 CA ALA A 312 229.643 7.244 96.601 1.00 74.48 C ANISOU 3085 CA ALA A 312 10649 7478 10172 -398 -147 762 C ATOM 3086 C ALA A 312 228.986 8.340 95.774 1.00 74.80 C ANISOU 3086 C ALA A 312 10570 7647 10205 -387 29 750 C ATOM 3087 O ALA A 312 228.741 8.161 94.576 1.00 79.05 O ANISOU 3087 O ALA A 312 11040 8214 10780 -343 55 712 O ATOM 3088 CB ALA A 312 228.593 6.458 97.385 1.00 74.89 C ANISOU 3088 CB ALA A 312 10831 7484 10140 -554 -201 863 C ATOM 3089 N VAL A 313 228.699 9.485 96.396 1.00 71.67 N ANISOU 3089 N VAL A 313 10154 7318 9758 -420 132 774 N ATOM 3090 CA VAL A 313 228.106 10.602 95.666 1.00 71.82 C ANISOU 3090 CA VAL A 313 10089 7426 9773 -394 253 755 C ATOM 3091 C VAL A 313 229.036 11.065 94.551 1.00 75.58 C ANISOU 3091 C VAL A 313 10492 7921 10304 -321 261 699 C ATOM 3092 O VAL A 313 228.595 11.348 93.430 1.00 78.50 O ANISOU 3092 O VAL A 313 10804 8336 10686 -306 309 685 O ATOM 3093 CB VAL A 313 227.765 11.747 96.637 1.00 72.86 C ANISOU 3093 CB VAL A 313 10229 7607 9847 -417 317 765 C ATOM 3094 CG1 VAL A 313 227.391 13.006 95.872 1.00 75.60 C ANISOU 3094 CG1 VAL A 313 10520 8001 10202 -363 386 732 C ATOM 3095 CG2 VAL A 313 226.639 11.330 97.567 1.00 73.02 C ANISOU 3095 CG2 VAL A 313 10279 7684 9780 -514 333 796 C ATOM 3096 N VAL A 314 230.337 11.138 94.836 1.00 75.13 N ANISOU 3096 N VAL A 314 10429 7851 10265 -292 209 663 N ATOM 3097 CA VAL A 314 231.295 11.567 93.822 1.00 71.44 C ANISOU 3097 CA VAL A 314 9873 7458 9815 -262 218 596 C ATOM 3098 C VAL A 314 231.470 10.489 92.760 1.00 70.95 C ANISOU 3098 C VAL A 314 9744 7418 9796 -212 166 526 C ATOM 3099 O VAL A 314 231.510 10.782 91.559 1.00 71.02 O ANISOU 3099 O VAL A 314 9668 7518 9800 -219 211 488 O ATOM 3100 CB VAL A 314 232.637 11.937 94.480 1.00 68.86 C ANISOU 3100 CB VAL A 314 9537 7150 9477 -254 178 558 C ATOM 3101 CG1 VAL A 314 233.671 12.296 93.423 1.00 64.61 C ANISOU 3101 CG1 VAL A 314 8882 6742 8923 -258 186 473 C ATOM 3102 CG2 VAL A 314 232.449 13.085 95.457 1.00 71.06 C ANISOU 3102 CG2 VAL A 314 9882 7404 9712 -301 227 621 C ATOM 3103 N ILE A 315 231.571 9.226 93.181 1.00 69.11 N ANISOU 3103 N ILE A 315 9561 7099 9599 -168 53 504 N ATOM 3104 CA ILE A 315 231.823 8.145 92.233 1.00 66.54 C ANISOU 3104 CA ILE A 315 9180 6779 9322 -94 -31 409 C ATOM 3105 C ILE A 315 230.622 7.940 91.319 1.00 62.84 C ANISOU 3105 C ILE A 315 8701 6319 8854 -127 32 449 C ATOM 3106 O ILE A 315 230.775 7.735 90.109 1.00 63.78 O ANISOU 3106 O ILE A 315 8720 6520 8992 -90 42 371 O ATOM 3107 CB ILE A 315 232.198 6.853 92.983 1.00 65.17 C ANISOU 3107 CB ILE A 315 9108 6465 9190 -34 -218 378 C ATOM 3108 CG1 ILE A 315 233.561 7.006 93.665 1.00 67.92 C ANISOU 3108 CG1 ILE A 315 9433 6827 9545 30 -297 298 C ATOM 3109 CG2 ILE A 315 232.205 5.660 92.037 1.00 66.27 C ANISOU 3109 CG2 ILE A 315 9220 6573 9384 54 -334 279 C ATOM 3110 CD1 ILE A 315 233.925 5.846 94.566 1.00 67.77 C ANISOU 3110 CD1 ILE A 315 9549 6637 9563 88 -513 281 C ATOM 3111 N ALA A 316 229.410 8.004 91.876 1.00 63.27 N ANISOU 3111 N ALA A 316 8843 6319 8877 -202 78 559 N ATOM 3112 CA ALA A 316 228.216 7.788 91.064 1.00 61.43 C ANISOU 3112 CA ALA A 316 8594 6108 8638 -234 135 591 C ATOM 3113 C ALA A 316 228.073 8.861 89.993 1.00 62.50 C ANISOU 3113 C ALA A 316 8629 6354 8764 -233 249 575 C ATOM 3114 O ALA A 316 227.680 8.568 88.857 1.00 62.23 O ANISOU 3114 O ALA A 316 8537 6362 8744 -223 269 549 O ATOM 3115 CB ALA A 316 226.973 7.749 91.954 1.00 59.32 C ANISOU 3115 CB ALA A 316 8411 5816 8311 -330 169 688 C ATOM 3116 N PHE A 317 228.396 10.109 90.331 1.00 63.95 N ANISOU 3116 N PHE A 317 8807 6574 8915 -253 305 595 N ATOM 3117 CA PHE A 317 228.257 11.188 89.360 1.00 65.17 C ANISOU 3117 CA PHE A 317 8912 6804 9048 -277 373 598 C ATOM 3118 C PHE A 317 229.219 11.009 88.192 1.00 69.41 C ANISOU 3118 C PHE A 317 9347 7439 9586 -277 359 519 C ATOM 3119 O PHE A 317 228.867 11.293 87.041 1.00 71.39 O ANISOU 3119 O PHE A 317 9551 7755 9820 -310 396 518 O ATOM 3120 CB PHE A 317 228.481 12.536 90.042 1.00 64.68 C ANISOU 3120 CB PHE A 317 8898 6732 8947 -305 396 634 C ATOM 3121 CG PHE A 317 228.306 13.709 89.127 1.00 64.06 C ANISOU 3121 CG PHE A 317 8817 6688 8835 -346 420 654 C ATOM 3122 CD1 PHE A 317 227.045 14.215 88.867 1.00 61.99 C ANISOU 3122 CD1 PHE A 317 8587 6397 8568 -329 439 684 C ATOM 3123 CD2 PHE A 317 229.402 14.308 88.529 1.00 67.96 C ANISOU 3123 CD2 PHE A 317 9282 7252 9288 -415 406 637 C ATOM 3124 CE1 PHE A 317 226.878 15.294 88.027 1.00 62.72 C ANISOU 3124 CE1 PHE A 317 8712 6488 8631 -365 419 707 C ATOM 3125 CE2 PHE A 317 229.243 15.389 87.685 1.00 69.36 C ANISOU 3125 CE2 PHE A 317 9494 7445 9415 -492 397 676 C ATOM 3126 CZ PHE A 317 227.978 15.883 87.434 1.00 66.31 C ANISOU 3126 CZ PHE A 317 9170 6987 9040 -459 391 716 C ATOM 3127 N VAL A 318 230.432 10.532 88.464 1.00 69.82 N ANISOU 3127 N VAL A 318 9356 7525 9649 -243 299 438 N ATOM 3128 CA VAL A 318 231.414 10.366 87.398 1.00 72.30 C ANISOU 3128 CA VAL A 318 9535 7993 9943 -245 286 323 C ATOM 3129 C VAL A 318 231.156 9.083 86.617 1.00 73.58 C ANISOU 3129 C VAL A 318 9639 8164 10155 -170 236 239 C ATOM 3130 O VAL A 318 231.263 9.062 85.386 1.00 73.84 O ANISOU 3130 O VAL A 318 9563 8331 10161 -195 265 174 O ATOM 3131 CB VAL A 318 232.837 10.406 87.983 1.00 72.20 C ANISOU 3131 CB VAL A 318 9470 8051 9912 -224 233 233 C ATOM 3132 CG1 VAL A 318 233.867 10.123 86.904 1.00 75.04 C ANISOU 3132 CG1 VAL A 318 9651 8630 10232 -223 216 70 C ATOM 3133 CG2 VAL A 318 233.098 11.757 88.629 1.00 73.77 C ANISOU 3133 CG2 VAL A 318 9730 8248 10051 -318 281 319 C ATOM 3134 N VAL A 319 230.803 7.998 87.311 1.00 73.72 N ANISOU 3134 N VAL A 319 9738 8037 10234 -93 148 243 N ATOM 3135 CA VAL A 319 230.545 6.731 86.629 1.00 72.17 C ANISOU 3135 CA VAL A 319 9518 7813 10089 -19 67 164 C ATOM 3136 C VAL A 319 229.355 6.862 85.686 1.00 72.64 C ANISOU 3136 C VAL A 319 9568 7894 10136 -76 157 231 C ATOM 3137 O VAL A 319 229.341 6.280 84.593 1.00 71.28 O ANISOU 3137 O VAL A 319 9311 7794 9980 -43 140 145 O ATOM 3138 CB VAL A 319 230.334 5.606 87.660 1.00 68.21 C ANISOU 3138 CB VAL A 319 9160 7118 9639 35 -77 187 C ATOM 3139 CG1 VAL A 319 229.714 4.384 87.006 1.00 67.86 C ANISOU 3139 CG1 VAL A 319 9145 7000 9638 78 -167 153 C ATOM 3140 CG2 VAL A 319 231.654 5.239 88.313 1.00 70.23 C ANISOU 3140 CG2 VAL A 319 9405 7358 9920 132 -211 73 C ATOM 3141 N CYS A 320 228.352 7.647 86.079 1.00 74.50 N ANISOU 3141 N CYS A 320 9881 8083 10343 -153 246 367 N ATOM 3142 CA CYS A 320 227.115 7.736 85.315 1.00 74.74 C ANISOU 3142 CA CYS A 320 9910 8124 10363 -192 315 426 C ATOM 3143 C CYS A 320 227.163 8.768 84.194 1.00 69.78 C ANISOU 3143 C CYS A 320 9201 7619 9691 -246 395 425 C ATOM 3144 O CYS A 320 226.525 8.564 83.155 1.00 71.25 O ANISOU 3144 O CYS A 320 9345 7849 9876 -260 423 422 O ATOM 3145 CB CYS A 320 225.946 8.058 86.249 1.00 76.95 C ANISOU 3145 CB CYS A 320 10290 8326 10622 -236 355 537 C ATOM 3146 SG CYS A 320 225.539 6.741 87.428 1.00 78.32 S ANISOU 3146 SG CYS A 320 10583 8371 10804 -250 256 573 S ATOM 3147 N TRP A 321 227.899 9.866 84.364 1.00 66.67 N ANISOU 3147 N TRP A 321 8801 7280 9251 -296 417 436 N ATOM 3148 CA TRP A 321 227.820 10.974 83.423 1.00 68.71 C ANISOU 3148 CA TRP A 321 9038 7621 9446 -388 464 472 C ATOM 3149 C TRP A 321 229.107 11.263 82.662 1.00 71.88 C ANISOU 3149 C TRP A 321 9333 8199 9779 -468 459 392 C ATOM 3150 O TRP A 321 229.071 12.055 81.714 1.00 72.47 O ANISOU 3150 O TRP A 321 9395 8361 9779 -585 481 426 O ATOM 3151 CB TRP A 321 227.366 12.250 84.148 1.00 70.33 C ANISOU 3151 CB TRP A 321 9357 7739 9626 -420 474 570 C ATOM 3152 CG TRP A 321 225.944 12.174 84.613 1.00 69.48 C ANISOU 3152 CG TRP A 321 9314 7532 9552 -363 490 622 C ATOM 3153 CD1 TRP A 321 225.510 11.910 85.879 1.00 67.98 C ANISOU 3153 CD1 TRP A 321 9177 7269 9384 -316 489 639 C ATOM 3154 CD2 TRP A 321 224.768 12.353 83.814 1.00 69.96 C ANISOU 3154 CD2 TRP A 321 9377 7593 9611 -360 510 649 C ATOM 3155 NE1 TRP A 321 224.138 11.916 85.920 1.00 68.59 N ANISOU 3155 NE1 TRP A 321 9271 7330 9461 -292 514 662 N ATOM 3156 CE2 TRP A 321 223.657 12.186 84.666 1.00 69.28 C ANISOU 3156 CE2 TRP A 321 9327 7454 9542 -304 524 665 C ATOM 3157 CE3 TRP A 321 224.545 12.640 82.463 1.00 71.11 C ANISOU 3157 CE3 TRP A 321 9492 7794 9731 -410 512 656 C ATOM 3158 CZ2 TRP A 321 222.343 12.297 84.211 1.00 69.64 C ANISOU 3158 CZ2 TRP A 321 9366 7511 9585 -278 541 671 C ATOM 3159 CZ3 TRP A 321 223.239 12.749 82.013 1.00 69.91 C ANISOU 3159 CZ3 TRP A 321 9355 7619 9589 -378 520 679 C ATOM 3160 CH2 TRP A 321 222.155 12.578 82.886 1.00 70.02 C ANISOU 3160 CH2 TRP A 321 9391 7589 9624 -303 535 678 C ATOM 3161 N LEU A 322 230.239 10.658 83.035 1.00 75.28 N ANISOU 3161 N LEU A 322 9684 8701 10217 -420 420 279 N ATOM 3162 CA LEU A 322 231.445 10.845 82.228 1.00 75.93 C ANISOU 3162 CA LEU A 322 9619 9020 10211 -504 422 165 C ATOM 3163 C LEU A 322 231.320 10.206 80.852 1.00 81.94 C ANISOU 3163 C LEU A 322 10250 9931 10952 -514 435 70 C ATOM 3164 O LEU A 322 231.559 10.903 79.850 1.00 81.91 O ANISOU 3164 O LEU A 322 10184 10101 10837 -674 474 75 O ATOM 3165 CB LEU A 322 232.675 10.336 82.985 1.00 76.50 C ANISOU 3165 CB LEU A 322 9616 9153 10296 -423 363 33 C ATOM 3166 CG LEU A 322 234.001 10.375 82.222 1.00 79.39 C ANISOU 3166 CG LEU A 322 9782 9824 10559 -493 361 -140 C ATOM 3167 CD1 LEU A 322 234.339 11.778 81.753 1.00 76.89 C ANISOU 3167 CD1 LEU A 322 9471 9650 10092 -731 422 -53 C ATOM 3168 CD2 LEU A 322 235.113 9.829 83.100 1.00 82.73 C ANISOU 3168 CD2 LEU A 322 10136 10285 11011 -372 283 -285 C ATOM 3169 N PRO A 323 230.960 8.923 80.712 1.00 83.32 N ANISOU 3169 N PRO A 323 10390 10051 11217 -371 391 -14 N ATOM 3170 CA PRO A 323 230.843 8.361 79.356 1.00 82.12 C ANISOU 3170 CA PRO A 323 10108 10052 11042 -382 403 -115 C ATOM 3171 C PRO A 323 229.822 9.082 78.496 1.00 79.52 C ANISOU 3171 C PRO A 323 9834 9714 10666 -508 476 23 C ATOM 3172 O PRO A 323 230.012 9.176 77.276 1.00 76.66 O ANISOU 3172 O PRO A 323 9356 9549 10221 -607 506 -36 O ATOM 3173 CB PRO A 323 230.442 6.902 79.616 1.00 79.89 C ANISOU 3173 CB PRO A 323 9847 9626 10881 -198 315 -192 C ATOM 3174 CG PRO A 323 230.905 6.621 81.003 1.00 80.26 C ANISOU 3174 CG PRO A 323 9980 9528 10987 -102 234 -195 C ATOM 3175 CD PRO A 323 230.683 7.901 81.739 1.00 80.81 C ANISOU 3175 CD PRO A 323 10159 9533 11012 -214 310 -24 C ATOM 3176 N TYR A 324 228.752 9.609 79.099 1.00 81.29 N ANISOU 3176 N TYR A 324 10224 9731 10932 -508 495 191 N ATOM 3177 CA TYR A 324 227.733 10.321 78.332 1.00 82.34 C ANISOU 3177 CA TYR A 324 10419 9837 11029 -598 534 308 C ATOM 3178 C TYR A 324 228.312 11.568 77.671 1.00 82.69 C ANISOU 3178 C TYR A 324 10461 10015 10941 -792 542 353 C ATOM 3179 O TYR A 324 228.143 11.782 76.466 1.00 86.04 O ANISOU 3179 O TYR A 324 10842 10559 11291 -908 556 360 O ATOM 3180 CB TYR A 324 226.559 10.689 79.239 1.00 81.10 C ANISOU 3180 CB TYR A 324 10417 9463 10934 -537 535 435 C ATOM 3181 CG TYR A 324 225.467 11.481 78.554 1.00 82.87 C ANISOU 3181 CG TYR A 324 10712 9645 11132 -594 547 534 C ATOM 3182 CD1 TYR A 324 224.498 10.846 77.788 1.00 83.11 C ANISOU 3182 CD1 TYR A 324 10710 9675 11193 -560 568 530 C ATOM 3183 CD2 TYR A 324 225.403 12.865 78.674 1.00 85.79 C ANISOU 3183 CD2 TYR A 324 11190 9960 11445 -675 514 625 C ATOM 3184 CE1 TYR A 324 223.494 11.565 77.162 1.00 83.86 C ANISOU 3184 CE1 TYR A 324 10866 9731 11265 -595 562 608 C ATOM 3185 CE2 TYR A 324 224.404 13.593 78.049 1.00 87.28 C ANISOU 3185 CE2 TYR A 324 11460 10088 11615 -703 483 700 C ATOM 3186 CZ TYR A 324 223.453 12.936 77.295 1.00 86.97 C ANISOU 3186 CZ TYR A 324 11373 10062 11608 -658 511 688 C ATOM 3187 OH TYR A 324 222.457 13.653 76.672 1.00 88.03 O ANISOU 3187 OH TYR A 324 11584 10138 11727 -672 466 750 O ATOM 3188 N HIS A 325 229.003 12.406 78.448 1.00 80.10 N ANISOU 3188 N HIS A 325 10195 9670 10570 -851 522 392 N ATOM 3189 CA HIS A 325 229.594 13.608 77.872 1.00 77.51 C ANISOU 3189 CA HIS A 325 9896 9460 10095 -1074 505 450 C ATOM 3190 C HIS A 325 230.752 13.276 76.941 1.00 80.54 C ANISOU 3190 C HIS A 325 10082 10164 10355 -1207 529 311 C ATOM 3191 O HIS A 325 230.991 14.005 75.971 1.00 83.24 O ANISOU 3191 O HIS A 325 10419 10659 10548 -1436 522 354 O ATOM 3192 CB HIS A 325 230.052 14.554 78.981 1.00 78.16 C ANISOU 3192 CB HIS A 325 10100 9438 10158 -1107 468 522 C ATOM 3193 CG HIS A 325 228.925 15.171 79.749 1.00 82.50 C ANISOU 3193 CG HIS A 325 10837 9721 10789 -1012 431 644 C ATOM 3194 ND1 HIS A 325 228.253 14.505 80.751 1.00 84.59 N ANISOU 3194 ND1 HIS A 325 11121 9840 11181 -817 452 629 N ATOM 3195 CD2 HIS A 325 228.347 16.392 79.657 1.00 87.51 C ANISOU 3195 CD2 HIS A 325 11642 10223 11385 -1087 358 763 C ATOM 3196 CE1 HIS A 325 227.312 15.289 81.246 1.00 87.04 C ANISOU 3196 CE1 HIS A 325 11573 9977 11519 -771 414 716 C ATOM 3197 NE2 HIS A 325 227.348 16.440 80.599 1.00 88.38 N ANISOU 3197 NE2 HIS A 325 11842 10137 11603 -911 346 791 N ATOM 3198 N VAL A 326 231.475 12.185 77.210 1.00 79.43 N ANISOU 3198 N VAL A 326 9778 10139 10264 -1073 540 133 N ATOM 3199 CA VAL A 326 232.573 11.785 76.333 1.00 74.76 C ANISOU 3199 CA VAL A 326 8955 9898 9553 -1165 557 -55 C ATOM 3200 C VAL A 326 232.046 11.397 74.957 1.00 74.97 C ANISOU 3200 C VAL A 326 8894 10053 9539 -1223 585 -91 C ATOM 3201 O VAL A 326 232.660 11.712 73.930 1.00 73.10 O ANISOU 3201 O VAL A 326 8526 10120 9131 -1434 608 -157 O ATOM 3202 CB VAL A 326 233.381 10.643 76.977 1.00 75.74 C ANISOU 3202 CB VAL A 326 8934 10083 9762 -952 523 -267 C ATOM 3203 CG1 VAL A 326 234.248 9.946 75.939 1.00 76.37 C ANISOU 3203 CG1 VAL A 326 8741 10527 9749 -970 526 -520 C ATOM 3204 CG2 VAL A 326 234.241 11.177 78.109 1.00 76.20 C ANISOU 3204 CG2 VAL A 326 9029 10123 9800 -962 500 -259 C ATOM 3205 N ARG A 327 230.899 10.712 74.914 1.00 79.57 N ANISOU 3205 N ARG A 327 9546 10427 10261 -1059 583 -49 N ATOM 3206 CA ARG A 327 230.310 10.324 73.636 1.00 78.60 C ANISOU 3206 CA ARG A 327 9351 10405 10110 -1104 608 -75 C ATOM 3207 C ARG A 327 229.971 11.544 72.791 1.00 78.68 C ANISOU 3207 C ARG A 327 9454 10464 9977 -1366 618 86 C ATOM 3208 O ARG A 327 230.254 11.574 71.587 1.00 80.45 O ANISOU 3208 O ARG A 327 9556 10946 10065 -1537 640 27 O ATOM 3209 CB ARG A 327 229.060 9.477 73.867 1.00 74.78 C ANISOU 3209 CB ARG A 327 8954 9665 9794 -901 599 -31 C ATOM 3210 CG ARG A 327 228.321 9.116 72.589 1.00 71.80 C ANISOU 3210 CG ARG A 327 8523 9360 9396 -942 626 -39 C ATOM 3211 CD ARG A 327 226.985 8.449 72.882 1.00 71.16 C ANISOU 3211 CD ARG A 327 8552 9024 9461 -779 618 35 C ATOM 3212 NE ARG A 327 226.133 9.271 73.738 1.00 69.12 N ANISOU 3212 NE ARG A 327 8488 8527 9247 -772 615 220 N ATOM 3213 CZ ARG A 327 225.412 10.302 73.309 1.00 67.71 C ANISOU 3213 CZ ARG A 327 8417 8295 9017 -883 617 362 C ATOM 3214 NH1 ARG A 327 225.438 10.646 72.029 1.00 68.25 N ANISOU 3214 NH1 ARG A 327 8434 8518 8979 -1039 624 369 N ATOM 3215 NH2 ARG A 327 224.667 10.993 74.160 1.00 65.58 N ANISOU 3215 NH2 ARG A 327 8304 7820 8793 -836 594 484 N ATOM 3216 N ARG A 328 229.365 12.563 73.404 1.00 77.26 N ANISOU 3216 N ARG A 328 9496 10040 9817 -1403 582 282 N ATOM 3217 CA ARG A 328 229.018 13.767 72.658 1.00 78.39 C ANISOU 3217 CA ARG A 328 9776 10175 9832 -1641 539 442 C ATOM 3218 C ARG A 328 230.260 14.512 72.188 1.00 79.69 C ANISOU 3218 C ARG A 328 9881 10619 9779 -1940 525 425 C ATOM 3219 O ARG A 328 230.220 15.191 71.156 1.00 82.76 O ANISOU 3219 O ARG A 328 10316 11122 10008 -2200 490 508 O ATOM 3220 CB ARG A 328 228.134 14.673 73.513 1.00 80.21 C ANISOU 3220 CB ARG A 328 10257 10074 10144 -1572 469 615 C ATOM 3221 CG ARG A 328 227.076 13.910 74.292 1.00 83.43 C ANISOU 3221 CG ARG A 328 10695 10258 10746 -1288 495 605 C ATOM 3222 CD ARG A 328 225.771 14.679 74.373 1.00 86.45 C ANISOU 3222 CD ARG A 328 11268 10402 11177 -1242 429 742 C ATOM 3223 NE ARG A 328 225.905 15.895 75.166 1.00 88.93 N ANISOU 3223 NE ARG A 328 11757 10565 11466 -1283 342 837 N ATOM 3224 CZ ARG A 328 224.963 16.826 75.261 1.00 89.85 C ANISOU 3224 CZ ARG A 328 12056 10480 11602 -1252 239 935 C ATOM 3225 NH1 ARG A 328 223.817 16.681 74.609 1.00 87.63 N ANISOU 3225 NH1 ARG A 328 11794 10138 11363 -1183 220 954 N ATOM 3226 NH2 ARG A 328 225.170 17.903 76.006 1.00 92.98 N ANISOU 3226 NH2 ARG A 328 12614 10738 11978 -1277 140 1000 N ATOM 3227 N LEU A 329 231.369 14.395 72.922 1.00 79.69 N ANISOU 3227 N LEU A 329 9781 10743 9753 -1927 545 319 N ATOM 3228 CA LEU A 329 232.620 14.986 72.458 1.00 77.78 C ANISOU 3228 CA LEU A 329 9438 10835 9279 -2228 545 270 C ATOM 3229 C LEU A 329 233.142 14.261 71.224 1.00 80.92 C ANISOU 3229 C LEU A 329 9564 11633 9548 -2336 606 80 C ATOM 3230 O LEU A 329 233.654 14.897 70.296 1.00 83.72 O ANISOU 3230 O LEU A 329 9875 12270 9667 -2675 600 102 O ATOM 3231 CB LEU A 329 233.657 14.968 73.580 1.00 74.26 C ANISOU 3231 CB LEU A 329 8929 10440 8845 -2162 552 178 C ATOM 3232 CG LEU A 329 233.332 15.840 74.794 1.00 71.14 C ANISOU 3232 CG LEU A 329 8790 9705 8534 -2108 490 355 C ATOM 3233 CD1 LEU A 329 234.278 15.539 75.943 1.00 70.23 C ANISOU 3233 CD1 LEU A 329 8588 9632 8465 -1984 508 240 C ATOM 3234 CD2 LEU A 329 233.379 17.315 74.428 1.00 72.90 C ANISOU 3234 CD2 LEU A 329 9221 9898 8579 -2435 402 550 C ATOM 3235 N MET A 330 233.021 12.930 71.197 1.00 80.98 N ANISOU 3235 N MET A 330 9394 11678 9698 -2062 650 -111 N ATOM 3236 CA MET A 330 233.364 12.173 69.996 1.00 83.44 C ANISOU 3236 CA MET A 330 9445 12348 9909 -2119 695 -313 C ATOM 3237 C MET A 330 232.564 12.653 68.796 1.00 86.42 C ANISOU 3237 C MET A 330 9910 12741 10185 -2336 694 -167 C ATOM 3238 O MET A 330 233.088 12.731 67.678 1.00 90.32 O ANISOU 3238 O MET A 330 10237 13613 10468 -2590 723 -256 O ATOM 3239 CB MET A 330 233.105 10.683 70.221 1.00 86.73 C ANISOU 3239 CB MET A 330 9733 12690 10531 -1755 699 -508 C ATOM 3240 CG MET A 330 234.292 9.876 70.699 1.00 89.22 C ANISOU 3240 CG MET A 330 9815 13225 10860 -1593 684 -795 C ATOM 3241 SD MET A 330 233.866 8.124 70.786 1.00 92.64 S ANISOU 3241 SD MET A 330 10153 13520 11525 -1186 629 -1008 S ATOM 3242 CE MET A 330 234.350 7.563 69.159 1.00 93.26 C ANISOU 3242 CE MET A 330 9907 14088 11438 -1290 662 -1282 C ATOM 3243 N PHE A 331 231.289 12.979 69.014 1.00 83.88 N ANISOU 3243 N PHE A 331 9841 12031 10001 -2243 655 47 N ATOM 3244 CA PHE A 331 230.395 13.313 67.912 1.00 79.94 C ANISOU 3244 CA PHE A 331 9432 11501 9439 -2391 636 176 C ATOM 3245 C PHE A 331 230.882 14.538 67.148 1.00 82.80 C ANISOU 3245 C PHE A 331 9874 12055 9531 -2819 583 304 C ATOM 3246 O PHE A 331 230.777 14.593 65.917 1.00 89.44 O ANISOU 3246 O PHE A 331 10656 13108 10220 -3039 587 308 O ATOM 3247 CB PHE A 331 228.982 13.533 68.458 1.00 75.80 C ANISOU 3247 CB PHE A 331 9162 10530 9110 -2195 586 362 C ATOM 3248 CG PHE A 331 227.981 13.953 67.423 1.00 73.24 C ANISOU 3248 CG PHE A 331 8957 10131 8739 -2317 541 502 C ATOM 3249 CD1 PHE A 331 227.264 13.007 66.714 1.00 71.87 C ANISOU 3249 CD1 PHE A 331 8678 9986 8644 -2189 592 426 C ATOM 3250 CD2 PHE A 331 227.740 15.295 67.175 1.00 76.40 C ANISOU 3250 CD2 PHE A 331 9597 10412 9021 -2555 424 709 C ATOM 3251 CE1 PHE A 331 226.336 13.389 65.768 1.00 74.38 C ANISOU 3251 CE1 PHE A 331 9105 10236 8921 -2296 546 552 C ATOM 3252 CE2 PHE A 331 226.816 15.684 66.227 1.00 78.45 C ANISOU 3252 CE2 PHE A 331 9983 10585 9241 -2656 354 833 C ATOM 3253 CZ PHE A 331 226.112 14.730 65.522 1.00 78.32 C ANISOU 3253 CZ PHE A 331 9839 10617 9301 -2526 424 754 C ATOM 3254 N CYS A 332 231.434 15.524 67.855 1.00 82.46 N ANISOU 3254 N CYS A 332 9975 11945 9410 -2963 522 413 N ATOM 3255 CA CYS A 332 231.773 16.802 67.250 1.00 89.28 C ANISOU 3255 CA CYS A 332 10997 12907 10018 -3390 427 584 C ATOM 3256 C CYS A 332 233.267 17.025 67.057 1.00 94.97 C ANISOU 3256 C CYS A 332 11526 14081 10478 -3701 465 463 C ATOM 3257 O CYS A 332 233.643 17.937 66.311 1.00104.02 O ANISOU 3257 O CYS A 332 12760 15410 11355 -4130 394 582 O ATOM 3258 CB CYS A 332 231.199 17.950 68.093 1.00 94.36 C ANISOU 3258 CB CYS A 332 11999 13117 10737 -3375 284 823 C ATOM 3259 SG CYS A 332 231.792 17.975 69.797 1.00 96.93 S ANISOU 3259 SG CYS A 332 12338 13287 11203 -3145 306 772 S ATOM 3260 N TYR A 333 234.126 16.228 67.691 1.00 91.28 N ANISOU 3260 N TYR A 333 10805 13810 10068 -3513 559 228 N ATOM 3261 CA TYR A 333 235.563 16.461 67.610 1.00 87.60 C ANISOU 3261 CA TYR A 333 10135 13796 9351 -3788 594 87 C ATOM 3262 C TYR A 333 236.273 15.581 66.593 1.00 92.17 C ANISOU 3262 C TYR A 333 10325 14924 9773 -3872 694 -206 C ATOM 3263 O TYR A 333 237.301 15.997 66.048 1.00102.33 O ANISOU 3263 O TYR A 333 11449 16677 10755 -4247 714 -290 O ATOM 3264 CB TYR A 333 236.214 16.274 68.985 1.00 85.77 C ANISOU 3264 CB TYR A 333 9862 13477 9251 -3553 612 -9 C ATOM 3265 CG TYR A 333 236.344 17.571 69.744 1.00 85.87 C ANISOU 3265 CG TYR A 333 10168 13255 9203 -3739 514 229 C ATOM 3266 CD1 TYR A 333 237.107 18.613 69.235 1.00 95.91 C ANISOU 3266 CD1 TYR A 333 11491 14794 10157 -4224 460 322 C ATOM 3267 CD2 TYR A 333 235.696 17.763 70.958 1.00 80.53 C ANISOU 3267 CD2 TYR A 333 9723 12101 8772 -3450 464 356 C ATOM 3268 CE1 TYR A 333 237.231 19.805 69.914 1.00 98.85 C ANISOU 3268 CE1 TYR A 333 12155 14931 10471 -4400 344 540 C ATOM 3269 CE2 TYR A 333 235.814 18.957 71.647 1.00 83.00 C ANISOU 3269 CE2 TYR A 333 10304 12197 9033 -3605 360 553 C ATOM 3270 CZ TYR A 333 236.583 19.974 71.118 1.00 90.86 C ANISOU 3270 CZ TYR A 333 11365 13432 9725 -4073 292 647 C ATOM 3271 OH TYR A 333 236.713 21.167 71.787 1.00 89.86 O ANISOU 3271 OH TYR A 333 11528 13072 9542 -4234 163 844 O ATOM 3272 N ILE A 334 235.763 14.385 66.319 1.00 83.40 N ANISOU 3272 N ILE A 334 9054 13788 8844 -3546 749 -376 N ATOM 3273 CA ILE A 334 236.338 13.538 65.280 1.00 79.64 C ANISOU 3273 CA ILE A 334 8211 13822 8228 -3600 826 -673 C ATOM 3274 C ILE A 334 235.854 14.070 63.934 1.00 82.56 C ANISOU 3274 C ILE A 334 8646 14337 8387 -3968 816 -528 C ATOM 3275 O ILE A 334 234.693 13.884 63.563 1.00 81.98 O ANISOU 3275 O ILE A 334 8727 13961 8458 -3844 794 -394 O ATOM 3276 CB ILE A 334 235.955 12.067 65.473 1.00 80.52 C ANISOU 3276 CB ILE A 334 8160 13822 8613 -3118 854 -905 C ATOM 3277 CG1 ILE A 334 236.293 11.610 66.894 1.00 75.18 C ANISOU 3277 CG1 ILE A 334 7497 12913 8156 -2765 828 -991 C ATOM 3278 CG2 ILE A 334 236.671 11.193 64.456 1.00 86.03 C ANISOU 3278 CG2 ILE A 334 8455 15071 9162 -3145 912 -1263 C ATOM 3279 CD1 ILE A 334 235.993 10.153 67.152 1.00 72.53 C ANISOU 3279 CD1 ILE A 334 7037 12446 8074 -2314 813 -1213 C ATOM 3280 N SER A 335 236.743 14.742 63.205 1.00 87.91 N ANISOU 3280 N SER A 335 9208 15488 8708 -4443 825 -552 N ATOM 3281 CA SER A 335 236.370 15.388 61.954 1.00 95.24 C ANISOU 3281 CA SER A 335 10235 16562 9391 -4869 790 -381 C ATOM 3282 C SER A 335 236.041 14.341 60.890 1.00101.77 C ANISOU 3282 C SER A 335 10799 17640 10228 -4759 869 -595 C ATOM 3283 O SER A 335 236.182 13.133 61.096 1.00105.41 O ANISOU 3283 O SER A 335 10998 18183 10871 -4367 937 -890 O ATOM 3284 CB SER A 335 237.487 16.316 61.483 1.00 96.76 C ANISOU 3284 CB SER A 335 10377 17221 9166 -5414 766 -366 C ATOM 3285 OG SER A 335 237.689 17.376 62.402 1.00 98.11 O ANISOU 3285 OG SER A 335 10833 17125 9321 -5562 673 -130 O ATOM 3286 N ASP A 336 235.605 14.828 59.723 1.00103.39 N ANISOU 3286 N ASP A 336 11093 17961 10229 -5121 838 -442 N ATOM 3287 CA ASP A 336 235.137 13.937 58.664 1.00106.36 C ANISOU 3287 CA ASP A 336 11270 18525 10618 -5032 901 -601 C ATOM 3288 C ASP A 336 236.225 12.966 58.223 1.00108.44 C ANISOU 3288 C ASP A 336 11108 19346 10748 -4904 984 -1045 C ATOM 3289 O ASP A 336 235.938 11.810 57.889 1.00105.93 O ANISOU 3289 O ASP A 336 10544 19119 10585 -4618 1050 -1286 O ATOM 3290 CB ASP A 336 234.650 14.757 57.468 1.00109.79 C ANISOU 3290 CB ASP A 336 11970 18935 10810 -5365 790 -367 C ATOM 3291 CG ASP A 336 233.578 15.758 57.845 1.00112.63 C ANISOU 3291 CG ASP A 336 12775 18728 11293 -5461 660 48 C ATOM 3292 OD1 ASP A 336 232.400 15.360 57.959 1.00113.73 O ANISOU 3292 OD1 ASP A 336 13026 18476 11709 -5185 660 144 O ATOM 3293 OD2 ASP A 336 233.914 16.947 58.027 1.00120.07 O ANISOU 3293 OD2 ASP A 336 13997 19571 12054 -5733 520 256 O ATOM 3294 N GLU A 337 237.481 13.412 58.227 1.00115.53 N ANISOU 3294 N GLU A 337 11925 20618 11353 -5101 967 -1172 N ATOM 3295 CA GLU A 337 238.564 12.615 57.663 1.00117.18 C ANISOU 3295 CA GLU A 337 11761 21398 11365 -5017 1026 -1604 C ATOM 3296 C GLU A 337 238.951 11.429 58.538 1.00119.96 C ANISOU 3296 C GLU A 337 11787 21794 11997 -4557 1087 -1950 C ATOM 3297 O GLU A 337 239.609 10.507 58.044 1.00126.08 O ANISOU 3297 O GLU A 337 12249 22964 12692 -4372 1115 -2347 O ATOM 3298 CB GLU A 337 239.790 13.496 57.427 1.00118.19 C ANISOU 3298 CB GLU A 337 11914 21931 11063 -5385 990 -1634 C ATOM 3299 CG GLU A 337 240.111 14.422 58.587 1.00115.54 C ANISOU 3299 CG GLU A 337 11779 21363 10758 -5502 942 -1416 C ATOM 3300 CD GLU A 337 241.096 15.507 58.210 1.00119.26 C ANISOU 3300 CD GLU A 337 12371 22170 10772 -5949 876 -1349 C ATOM 3301 OE1 GLU A 337 241.676 15.430 57.106 1.00121.61 O ANISOU 3301 OE1 GLU A 337 12540 22954 10711 -6148 889 -1528 O ATOM 3302 OE2 GLU A 337 241.290 16.438 59.019 1.00120.92 O ANISOU 3302 OE2 GLU A 337 12811 22167 10967 -6107 807 -1122 O ATOM 3303 N GLN A 338 238.568 11.424 59.815 1.00115.53 N ANISOU 3303 N GLN A 338 11303 20840 11753 -4362 1088 -1823 N ATOM 3304 CA GLN A 338 238.989 10.367 60.724 1.00112.08 C ANISOU 3304 CA GLN A 338 10615 20397 11572 -3904 1098 -2138 C ATOM 3305 C GLN A 338 237.927 9.301 60.958 1.00108.34 C ANISOU 3305 C GLN A 338 10250 19438 11477 -3400 1059 -2150 C ATOM 3306 O GLN A 338 238.246 8.256 61.535 1.00111.79 O ANISOU 3306 O GLN A 338 10524 19835 12115 -2973 1020 -2435 O ATOM 3307 CB GLN A 338 239.411 10.958 62.077 1.00116.60 C ANISOU 3307 CB GLN A 338 11369 20703 12229 -3845 1057 -2003 C ATOM 3308 CG GLN A 338 240.577 11.933 62.009 1.00120.30 C ANISOU 3308 CG GLN A 338 11755 21622 12333 -4290 1075 -2014 C ATOM 3309 CD GLN A 338 240.143 13.371 62.210 1.00121.74 C ANISOU 3309 CD GLN A 338 12352 21492 12411 -4679 1026 -1550 C ATOM 3310 OE1 GLN A 338 238.991 13.640 62.546 1.00125.11 O ANISOU 3310 OE1 GLN A 338 13123 21345 13068 -4564 977 -1239 O ATOM 3311 NE2 GLN A 338 241.068 14.304 62.011 1.00125.23 N ANISOU 3311 NE2 GLN A 338 12879 22202 12499 -5026 987 -1503 N ATOM 3312 N TRP A 339 236.686 9.525 60.533 1.00101.91 N ANISOU 3312 N TRP A 339 9710 18258 10755 -3443 1051 -1855 N ATOM 3313 CA TRP A 339 235.609 8.570 60.786 1.00 99.83 C ANISOU 3313 CA TRP A 339 9571 17529 10833 -3005 1015 -1837 C ATOM 3314 C TRP A 339 235.723 7.408 59.810 1.00 99.65 C ANISOU 3314 C TRP A 339 9219 17851 10793 -2855 1035 -2191 C ATOM 3315 O TRP A 339 235.345 7.518 58.642 1.00103.74 O ANISOU 3315 O TRP A 339 9682 18577 11157 -3091 1079 -2160 O ATOM 3316 CB TRP A 339 234.246 9.243 60.678 1.00 98.01 C ANISOU 3316 CB TRP A 339 9726 16819 10694 -3101 995 -1421 C ATOM 3317 CG TRP A 339 233.852 9.998 61.909 1.00 95.55 C ANISOU 3317 CG TRP A 339 9758 16015 10534 -3034 943 -1124 C ATOM 3318 CD1 TRP A 339 234.054 11.321 62.154 1.00 97.30 C ANISOU 3318 CD1 TRP A 339 10184 16189 10596 -3365 914 -872 C ATOM 3319 CD2 TRP A 339 233.197 9.471 63.071 1.00 90.14 C ANISOU 3319 CD2 TRP A 339 9249 14825 10175 -2622 900 -1061 C ATOM 3320 NE1 TRP A 339 233.557 11.658 63.390 1.00 92.87 N ANISOU 3320 NE1 TRP A 339 9902 15129 10254 -3158 861 -672 N ATOM 3321 CE2 TRP A 339 233.030 10.537 63.976 1.00 87.91 C ANISOU 3321 CE2 TRP A 339 9252 14233 9916 -2714 861 -783 C ATOM 3322 CE3 TRP A 339 232.735 8.202 63.432 1.00 86.15 C ANISOU 3322 CE3 TRP A 339 8698 14105 9930 -2205 878 -1210 C ATOM 3323 CZ2 TRP A 339 232.421 10.375 65.217 1.00 82.88 C ANISOU 3323 CZ2 TRP A 339 8825 13121 9543 -2406 821 -665 C ATOM 3324 CZ3 TRP A 339 232.130 8.042 64.666 1.00 82.76 C ANISOU 3324 CZ3 TRP A 339 8499 13194 9752 -1930 830 -1070 C ATOM 3325 CH2 TRP A 339 231.979 9.123 65.543 1.00 81.13 C ANISOU 3325 CH2 TRP A 339 8546 12727 9555 -2032 812 -807 C ATOM 3326 N THR A 340 236.247 6.284 60.291 1.00 96.70 N ANISOU 3326 N THR A 340 8634 17527 10579 -2455 983 -2537 N ATOM 3327 CA THR A 340 236.242 5.053 59.521 1.00 97.52 C ANISOU 3327 CA THR A 340 8470 17850 10734 -2216 959 -2887 C ATOM 3328 C THR A 340 234.908 4.335 59.716 1.00 94.41 C ANISOU 3328 C THR A 340 8336 16881 10655 -1900 903 -2724 C ATOM 3329 O THR A 340 234.015 4.805 60.428 1.00 87.07 O ANISOU 3329 O THR A 340 7763 15436 9885 -1877 894 -2360 O ATOM 3330 CB THR A 340 237.413 4.161 59.928 1.00 99.18 C ANISOU 3330 CB THR A 340 8349 18360 10973 -1912 883 -3357 C ATOM 3331 OG1 THR A 340 237.251 3.748 61.291 1.00 98.73 O ANISOU 3331 OG1 THR A 340 8510 17789 11216 -1538 775 -3291 O ATOM 3332 CG2 THR A 340 238.730 4.910 59.785 1.00102.08 C ANISOU 3332 CG2 THR A 340 8444 19330 11011 -2244 948 -3522 C ATOM 3333 N THR A 341 234.765 3.176 59.069 1.00 96.89 N ANISOU 3333 N THR A 341 8461 17305 11047 -1659 857 -3010 N ATOM 3334 CA THR A 341 233.551 2.386 59.244 1.00 92.04 C ANISOU 3334 CA THR A 341 8078 16176 10716 -1367 791 -2884 C ATOM 3335 C THR A 341 233.439 1.848 60.664 1.00 93.03 C ANISOU 3335 C THR A 341 8404 15818 11123 -1002 670 -2849 C ATOM 3336 O THR A 341 232.332 1.758 61.208 1.00 94.54 O ANISOU 3336 O THR A 341 8910 15497 11516 -891 645 -2565 O ATOM 3337 CB THR A 341 233.518 1.236 58.235 1.00 82.61 C ANISOU 3337 CB THR A 341 6633 15222 9533 -1191 747 -3226 C ATOM 3338 OG1 THR A 341 233.587 1.763 56.904 1.00 85.20 O ANISOU 3338 OG1 THR A 341 6777 16014 9580 -1563 867 -3244 O ATOM 3339 CG2 THR A 341 232.237 0.433 58.379 1.00 72.75 C ANISOU 3339 CG2 THR A 341 5637 13447 8556 -929 675 -3078 C ATOM 3340 N PHE A 342 234.571 1.504 61.285 1.00 93.33 N ANISOU 3340 N PHE A 342 8264 16031 11164 -827 589 -3136 N ATOM 3341 CA PHE A 342 234.532 0.954 62.635 1.00 95.29 C ANISOU 3341 CA PHE A 342 8707 15832 11667 -491 451 -3113 C ATOM 3342 C PHE A 342 234.111 2.004 63.655 1.00 93.97 C ANISOU 3342 C PHE A 342 8856 15308 11541 -642 513 -2700 C ATOM 3343 O PHE A 342 233.321 1.711 64.561 1.00 97.97 O ANISOU 3343 O PHE A 342 9647 15309 12266 -458 447 -2497 O ATOM 3344 CB PHE A 342 235.890 0.365 63.010 1.00 95.83 C ANISOU 3344 CB PHE A 342 8498 16194 11718 -264 330 -3540 C ATOM 3345 CG PHE A 342 235.951 -0.149 64.418 1.00 97.33 C ANISOU 3345 CG PHE A 342 8895 15937 12147 54 169 -3515 C ATOM 3346 CD1 PHE A 342 235.436 -1.394 64.737 1.00 96.17 C ANISOU 3346 CD1 PHE A 342 8885 15412 12243 412 -22 -3604 C ATOM 3347 CD2 PHE A 342 236.518 0.615 65.425 1.00 95.44 C ANISOU 3347 CD2 PHE A 342 8733 15652 11879 -25 194 -3391 C ATOM 3348 CE1 PHE A 342 235.486 -1.869 66.032 1.00 94.75 C ANISOU 3348 CE1 PHE A 342 8919 14818 12263 667 -190 -3564 C ATOM 3349 CE2 PHE A 342 236.571 0.146 66.723 1.00 93.27 C ANISOU 3349 CE2 PHE A 342 8653 14973 11812 249 42 -3361 C ATOM 3350 CZ PHE A 342 236.054 -1.099 67.027 1.00 92.75 C ANISOU 3350 CZ PHE A 342 8728 14536 11977 588 -153 -3443 C ATOM 3351 N LEU A 343 234.633 3.228 63.534 1.00 89.87 N ANISOU 3351 N LEU A 343 8291 15054 10799 -986 628 -2580 N ATOM 3352 CA LEU A 343 234.263 4.279 64.477 1.00 87.47 C ANISOU 3352 CA LEU A 343 8287 14419 10528 -1124 669 -2208 C ATOM 3353 C LEU A 343 232.774 4.593 64.411 1.00 84.30 C ANISOU 3353 C LEU A 343 8196 13596 10237 -1176 704 -1846 C ATOM 3354 O LEU A 343 232.184 5.017 65.412 1.00 85.52 O ANISOU 3354 O LEU A 343 8627 13346 10522 -1128 690 -1582 O ATOM 3355 CB LEU A 343 235.084 5.540 64.212 1.00 85.17 C ANISOU 3355 CB LEU A 343 7904 14503 9954 -1519 762 -2149 C ATOM 3356 CG LEU A 343 236.567 5.474 64.576 1.00 85.25 C ANISOU 3356 CG LEU A 343 7641 14906 9845 -1498 736 -2458 C ATOM 3357 CD1 LEU A 343 237.269 6.766 64.201 1.00 88.53 C ANISOU 3357 CD1 LEU A 343 7985 15707 9944 -1960 832 -2363 C ATOM 3358 CD2 LEU A 343 236.741 5.176 66.058 1.00 83.36 C ANISOU 3358 CD2 LEU A 343 7552 14296 9826 -1197 640 -2438 C ATOM 3359 N PHE A 344 232.150 4.386 63.249 1.00 82.74 N ANISOU 3359 N PHE A 344 7946 13508 9986 -1268 745 -1846 N ATOM 3360 CA PHE A 344 230.716 4.624 63.131 1.00 80.01 C ANISOU 3360 CA PHE A 344 7870 12788 9744 -1297 770 -1534 C ATOM 3361 C PHE A 344 229.925 3.559 63.879 1.00 78.63 C ANISOU 3361 C PHE A 344 7845 12190 9841 -948 683 -1526 C ATOM 3362 O PHE A 344 229.037 3.879 64.676 1.00 78.32 O ANISOU 3362 O PHE A 344 8073 11758 9928 -906 679 -1260 O ATOM 3363 CB PHE A 344 230.312 4.668 61.657 1.00 78.28 C ANISOU 3363 CB PHE A 344 7542 12820 9380 -1498 831 -1548 C ATOM 3364 CG PHE A 344 228.902 5.146 61.425 1.00 78.90 C ANISOU 3364 CG PHE A 344 7885 12571 9521 -1581 856 -1221 C ATOM 3365 CD1 PHE A 344 228.563 6.473 61.631 1.00 77.47 C ANISOU 3365 CD1 PHE A 344 7922 12254 9259 -1822 877 -919 C ATOM 3366 CD2 PHE A 344 227.919 4.269 60.995 1.00 79.19 C ANISOU 3366 CD2 PHE A 344 7955 12439 9695 -1412 841 -1233 C ATOM 3367 CE1 PHE A 344 227.270 6.915 61.413 1.00 75.31 C ANISOU 3367 CE1 PHE A 344 7879 11690 9045 -1868 875 -654 C ATOM 3368 CE2 PHE A 344 226.622 4.705 60.777 1.00 78.48 C ANISOU 3368 CE2 PHE A 344 8085 12077 9655 -1480 862 -956 C ATOM 3369 CZ PHE A 344 226.299 6.030 60.987 1.00 75.91 C ANISOU 3369 CZ PHE A 344 7961 11629 9253 -1696 876 -677 C ATOM 3370 N ASP A 345 230.238 2.283 63.641 1.00 79.24 N ANISOU 3370 N ASP A 345 7756 12351 9999 -702 597 -1825 N ATOM 3371 CA ASP A 345 229.521 1.214 64.330 1.00 80.61 C ANISOU 3371 CA ASP A 345 8098 12119 10412 -403 482 -1814 C ATOM 3372 C ASP A 345 229.789 1.248 65.828 1.00 78.99 C ANISOU 3372 C ASP A 345 8055 11630 10326 -263 407 -1738 C ATOM 3373 O ASP A 345 228.887 0.992 66.634 1.00 79.67 O ANISOU 3373 O ASP A 345 8388 11317 10565 -162 363 -1542 O ATOM 3374 CB ASP A 345 229.906 -0.145 63.747 1.00 82.97 C ANISOU 3374 CB ASP A 345 8199 12561 10765 -167 362 -2173 C ATOM 3375 CG ASP A 345 229.347 -0.361 62.356 1.00 83.96 C ANISOU 3375 CG ASP A 345 8212 12875 10813 -269 425 -2218 C ATOM 3376 OD1 ASP A 345 228.379 0.338 61.988 1.00 81.41 O ANISOU 3376 OD1 ASP A 345 8032 12447 10452 -471 535 -1929 O ATOM 3377 OD2 ASP A 345 229.872 -1.232 61.632 1.00 86.61 O ANISOU 3377 OD2 ASP A 345 8313 13467 11127 -136 352 -2556 O ATOM 3378 N PHE A 346 231.024 1.568 66.221 1.00 76.43 N ANISOU 3378 N PHE A 346 7587 11532 9920 -272 392 -1894 N ATOM 3379 CA PHE A 346 231.343 1.650 67.641 1.00 77.28 C ANISOU 3379 CA PHE A 346 7844 11390 10131 -152 321 -1824 C ATOM 3380 C PHE A 346 230.552 2.759 68.322 1.00 75.57 C ANISOU 3380 C PHE A 346 7886 10907 9921 -323 417 -1445 C ATOM 3381 O PHE A 346 230.026 2.567 69.423 1.00 76.74 O ANISOU 3381 O PHE A 346 8251 10695 10211 -202 361 -1297 O ATOM 3382 CB PHE A 346 232.845 1.866 67.831 1.00 81.11 C ANISOU 3382 CB PHE A 346 8099 12217 10503 -152 298 -2074 C ATOM 3383 CG PHE A 346 233.223 2.284 69.223 1.00 84.70 C ANISOU 3383 CG PHE A 346 8701 12463 11019 -106 262 -1959 C ATOM 3384 CD1 PHE A 346 233.268 1.357 70.251 1.00 84.37 C ANISOU 3384 CD1 PHE A 346 8780 12117 11161 179 94 -2027 C ATOM 3385 CD2 PHE A 346 233.534 3.605 69.503 1.00 83.64 C ANISOU 3385 CD2 PHE A 346 8603 12426 10751 -359 378 -1778 C ATOM 3386 CE1 PHE A 346 233.613 1.740 71.534 1.00 83.05 C ANISOU 3386 CE1 PHE A 346 8748 11766 11042 211 61 -1920 C ATOM 3387 CE2 PHE A 346 233.880 3.994 70.783 1.00 82.72 C ANISOU 3387 CE2 PHE A 346 8619 12121 10689 -315 345 -1679 C ATOM 3388 CZ PHE A 346 233.921 3.060 71.800 1.00 81.97 C ANISOU 3388 CZ PHE A 346 8625 11744 10777 -29 196 -1751 C ATOM 3389 N TYR A 347 230.450 3.925 67.675 1.00 74.41 N ANISOU 3389 N TYR A 347 7726 10937 9611 -610 543 -1295 N ATOM 3390 CA TYR A 347 229.756 5.061 68.276 1.00 73.87 C ANISOU 3390 CA TYR A 347 7898 10626 9541 -756 603 -968 C ATOM 3391 C TYR A 347 228.315 4.725 68.630 1.00 74.37 C ANISOU 3391 C TYR A 347 8185 10310 9764 -646 590 -773 C ATOM 3392 O TYR A 347 227.784 5.239 69.620 1.00 74.56 O ANISOU 3392 O TYR A 347 8409 10066 9855 -634 591 -574 O ATOM 3393 CB TYR A 347 229.800 6.263 67.330 1.00 73.02 C ANISOU 3393 CB TYR A 347 7763 10751 9229 -1084 693 -849 C ATOM 3394 CG TYR A 347 229.009 7.463 67.812 1.00 74.23 C ANISOU 3394 CG TYR A 347 8180 10641 9384 -1219 716 -530 C ATOM 3395 CD1 TYR A 347 229.597 8.425 68.622 1.00 79.78 C ANISOU 3395 CD1 TYR A 347 8969 11314 10029 -1321 710 -435 C ATOM 3396 CD2 TYR A 347 227.678 7.640 67.443 1.00 73.12 C ANISOU 3396 CD2 TYR A 347 8196 10287 9299 -1232 729 -345 C ATOM 3397 CE1 TYR A 347 228.880 9.523 69.063 1.00 81.02 C ANISOU 3397 CE1 TYR A 347 9369 11222 10192 -1418 702 -172 C ATOM 3398 CE2 TYR A 347 226.955 8.733 67.879 1.00 73.28 C ANISOU 3398 CE2 TYR A 347 8444 10076 9324 -1320 721 -95 C ATOM 3399 CZ TYR A 347 227.560 9.672 68.688 1.00 78.34 C ANISOU 3399 CZ TYR A 347 9175 10678 9914 -1406 700 -14 C ATOM 3400 OH TYR A 347 226.845 10.764 69.123 1.00 79.49 O ANISOU 3400 OH TYR A 347 9550 10584 10069 -1468 665 208 O ATOM 3401 N HIS A 348 227.666 3.873 67.840 1.00 74.43 N ANISOU 3401 N HIS A 348 8149 10312 9819 -573 577 -840 N ATOM 3402 CA HIS A 348 226.277 3.535 68.112 1.00 74.77 C ANISOU 3402 CA HIS A 348 8385 10039 9988 -496 570 -665 C ATOM 3403 C HIS A 348 226.151 2.437 69.159 1.00 76.62 C ANISOU 3403 C HIS A 348 8717 10015 10381 -267 456 -717 C ATOM 3404 O HIS A 348 225.184 2.432 69.928 1.00 76.86 O ANISOU 3404 O HIS A 348 8938 9772 10492 -240 451 -536 O ATOM 3405 CB HIS A 348 225.582 3.136 66.814 1.00 74.00 C ANISOU 3405 CB HIS A 348 8215 10039 9862 -541 602 -694 C ATOM 3406 CG HIS A 348 225.465 4.261 65.833 1.00 72.48 C ANISOU 3406 CG HIS A 348 7988 10040 9511 -794 694 -586 C ATOM 3407 ND1 HIS A 348 224.563 5.291 65.988 1.00 71.46 N ANISOU 3407 ND1 HIS A 348 8042 9742 9368 -911 732 -329 N ATOM 3408 CD2 HIS A 348 226.146 4.525 64.694 1.00 72.06 C ANISOU 3408 CD2 HIS A 348 7746 10339 9294 -963 734 -704 C ATOM 3409 CE1 HIS A 348 224.689 6.139 64.982 1.00 70.66 C ANISOU 3409 CE1 HIS A 348 7897 9842 9109 -1141 772 -278 C ATOM 3410 NE2 HIS A 348 225.644 5.697 64.183 1.00 71.06 N ANISOU 3410 NE2 HIS A 348 7721 10222 9055 -1199 784 -493 N ATOM 3411 N TYR A 349 227.104 1.504 69.209 1.00 77.37 N ANISOU 3411 N TYR A 349 8688 10200 10510 -110 346 -971 N ATOM 3412 CA TYR A 349 227.172 0.604 70.354 1.00 78.31 C ANISOU 3412 CA TYR A 349 8937 10054 10765 85 199 -1006 C ATOM 3413 C TYR A 349 227.596 1.360 71.607 1.00 78.81 C ANISOU 3413 C TYR A 349 9099 10017 10827 57 212 -889 C ATOM 3414 O TYR A 349 227.069 1.115 72.698 1.00 78.80 O ANISOU 3414 O TYR A 349 9293 9735 10913 111 155 -755 O ATOM 3415 CB TYR A 349 228.134 -0.551 70.074 1.00 79.14 C ANISOU 3415 CB TYR A 349 8891 10270 10911 288 36 -1334 C ATOM 3416 CG TYR A 349 227.577 -1.624 69.164 1.00 81.23 C ANISOU 3416 CG TYR A 349 9125 10514 11225 380 -39 -1451 C ATOM 3417 CD1 TYR A 349 226.585 -2.490 69.607 1.00 78.56 C ANISOU 3417 CD1 TYR A 349 9007 9840 11002 455 -145 -1338 C ATOM 3418 CD2 TYR A 349 228.063 -1.790 67.874 1.00 87.38 C ANISOU 3418 CD2 TYR A 349 9653 11626 11920 375 -12 -1682 C ATOM 3419 CE1 TYR A 349 226.077 -3.479 68.785 1.00 78.69 C ANISOU 3419 CE1 TYR A 349 9011 9826 11062 531 -228 -1442 C ATOM 3420 CE2 TYR A 349 227.563 -2.777 67.043 1.00 89.24 C ANISOU 3420 CE2 TYR A 349 9860 11842 12204 468 -88 -1801 C ATOM 3421 CZ TYR A 349 226.571 -3.619 67.504 1.00 85.39 C ANISOU 3421 CZ TYR A 349 9611 10990 11844 551 -200 -1676 C ATOM 3422 OH TYR A 349 226.071 -4.603 66.682 1.00 88.13 O ANISOU 3422 OH TYR A 349 9944 11306 12236 635 -288 -1790 O ATOM 3423 N PHE A 350 228.547 2.287 71.462 1.00 78.60 N ANISOU 3423 N PHE A 350 8940 10236 10687 -51 284 -938 N ATOM 3424 CA PHE A 350 228.940 3.145 72.574 1.00 79.04 C ANISOU 3424 CA PHE A 350 9090 10213 10729 -102 308 -817 C ATOM 3425 C PHE A 350 227.771 3.986 73.062 1.00 78.53 C ANISOU 3425 C PHE A 350 9231 9930 10677 -213 393 -522 C ATOM 3426 O PHE A 350 227.705 4.329 74.247 1.00 78.91 O ANISOU 3426 O PHE A 350 9417 9800 10767 -194 379 -407 O ATOM 3427 CB PHE A 350 230.103 4.039 72.140 1.00 78.25 C ANISOU 3427 CB PHE A 350 8808 10449 10474 -246 374 -914 C ATOM 3428 CG PHE A 350 230.751 4.800 73.260 1.00 78.73 C ANISOU 3428 CG PHE A 350 8936 10462 10516 -281 377 -842 C ATOM 3429 CD1 PHE A 350 231.312 4.135 74.337 1.00 80.04 C ANISOU 3429 CD1 PHE A 350 9137 10496 10780 -93 260 -940 C ATOM 3430 CD2 PHE A 350 230.837 6.182 73.214 1.00 77.78 C ANISOU 3430 CD2 PHE A 350 8854 10424 10273 -507 475 -681 C ATOM 3431 CE1 PHE A 350 231.923 4.835 75.361 1.00 80.60 C ANISOU 3431 CE1 PHE A 350 9263 10531 10830 -128 265 -877 C ATOM 3432 CE2 PHE A 350 231.448 6.887 74.233 1.00 77.95 C ANISOU 3432 CE2 PHE A 350 8940 10401 10275 -541 472 -620 C ATOM 3433 CZ PHE A 350 231.993 6.212 75.308 1.00 79.59 C ANISOU 3433 CZ PHE A 350 9163 10495 10582 -351 379 -720 C ATOM 3434 N TYR A 351 226.837 4.317 72.167 1.00 77.02 N ANISOU 3434 N TYR A 351 9054 9761 10449 -319 471 -417 N ATOM 3435 CA TYR A 351 225.681 5.119 72.553 1.00 75.16 C ANISOU 3435 CA TYR A 351 8992 9341 10224 -397 532 -177 C ATOM 3436 C TYR A 351 224.801 4.380 73.552 1.00 74.97 C ANISOU 3436 C TYR A 351 9120 9050 10315 -278 480 -101 C ATOM 3437 O TYR A 351 224.245 4.991 74.473 1.00 73.32 O ANISOU 3437 O TYR A 351 9042 8695 10120 -301 504 48 O ATOM 3438 CB TYR A 351 224.880 5.503 71.307 1.00 77.84 C ANISOU 3438 CB TYR A 351 9306 9767 10502 -514 598 -110 C ATOM 3439 CG TYR A 351 223.658 6.354 71.578 1.00 79.07 C ANISOU 3439 CG TYR A 351 9622 9756 10667 -569 638 100 C ATOM 3440 CD1 TYR A 351 223.756 7.737 71.662 1.00 81.67 C ANISOU 3440 CD1 TYR A 351 10020 10093 10917 -696 657 217 C ATOM 3441 CD2 TYR A 351 222.404 5.775 71.731 1.00 79.18 C ANISOU 3441 CD2 TYR A 351 9713 9614 10757 -495 637 164 C ATOM 3442 CE1 TYR A 351 222.641 8.519 71.903 1.00 82.51 C ANISOU 3442 CE1 TYR A 351 10267 10047 11038 -709 661 371 C ATOM 3443 CE2 TYR A 351 221.283 6.550 71.973 1.00 79.29 C ANISOU 3443 CE2 TYR A 351 9840 9516 10771 -524 665 313 C ATOM 3444 CZ TYR A 351 221.407 7.921 72.056 1.00 82.12 C ANISOU 3444 CZ TYR A 351 10260 9875 11065 -612 670 405 C ATOM 3445 OH TYR A 351 220.295 8.697 72.296 1.00 82.97 O ANISOU 3445 OH TYR A 351 10475 9870 11180 -605 666 517 O ATOM 3446 N MET A 352 224.661 3.065 73.387 1.00 76.72 N ANISOU 3446 N MET A 352 9329 9215 10608 -165 396 -207 N ATOM 3447 CA MET A 352 223.814 2.297 74.292 1.00 74.26 C ANISOU 3447 CA MET A 352 9178 8661 10375 -103 330 -123 C ATOM 3448 C MET A 352 224.386 2.278 75.703 1.00 73.72 C ANISOU 3448 C MET A 352 9206 8464 10340 -53 258 -105 C ATOM 3449 O MET A 352 223.645 2.425 76.681 1.00 75.93 O ANISOU 3449 O MET A 352 9627 8593 10631 -88 268 39 O ATOM 3450 CB MET A 352 223.645 0.873 73.765 1.00 74.16 C ANISOU 3450 CB MET A 352 9156 8600 10422 -9 217 -245 C ATOM 3451 CG MET A 352 222.904 0.776 72.443 1.00 74.90 C ANISOU 3451 CG MET A 352 9173 8798 10489 -60 286 -249 C ATOM 3452 SD MET A 352 222.957 -0.887 71.748 1.00 75.32 S ANISOU 3452 SD MET A 352 9197 8812 10609 70 129 -437 S ATOM 3453 CE MET A 352 221.857 -0.699 70.348 1.00 75.71 C ANISOU 3453 CE MET A 352 9176 8979 10611 -33 253 -378 C ATOM 3454 N LEU A 353 225.705 2.109 75.825 1.00 75.66 N ANISOU 3454 N LEU A 353 9365 8793 10590 25 186 -262 N ATOM 3455 CA LEU A 353 226.315 1.962 77.143 1.00 75.46 C ANISOU 3455 CA LEU A 353 9431 8637 10601 88 94 -261 C ATOM 3456 C LEU A 353 226.314 3.277 77.913 1.00 76.30 C ANISOU 3456 C LEU A 353 9586 8746 10658 -11 203 -114 C ATOM 3457 O LEU A 353 226.017 3.298 79.113 1.00 79.51 O ANISOU 3457 O LEU A 353 10133 8991 11088 -14 174 -9 O ATOM 3458 CB LEU A 353 227.740 1.425 77.000 1.00 76.90 C ANISOU 3458 CB LEU A 353 9485 8932 10801 220 -25 -502 C ATOM 3459 CG LEU A 353 228.596 1.369 78.268 1.00 76.67 C ANISOU 3459 CG LEU A 353 9523 8804 10802 295 -129 -531 C ATOM 3460 CD1 LEU A 353 227.976 0.435 79.296 1.00 76.45 C ANISOU 3460 CD1 LEU A 353 9722 8476 10849 341 -277 -437 C ATOM 3461 CD2 LEU A 353 230.020 0.944 77.939 1.00 78.34 C ANISOU 3461 CD2 LEU A 353 9558 9192 11016 436 -239 -810 C ATOM 3462 N THR A 354 226.642 4.385 77.244 1.00 76.11 N ANISOU 3462 N THR A 354 9459 8905 10555 -107 313 -105 N ATOM 3463 CA THR A 354 226.777 5.656 77.950 1.00 73.80 C ANISOU 3463 CA THR A 354 9224 8602 10214 -194 382 15 C ATOM 3464 C THR A 354 225.439 6.137 78.496 1.00 71.63 C ANISOU 3464 C THR A 354 9091 8175 9951 -237 434 196 C ATOM 3465 O THR A 354 225.373 6.677 79.607 1.00 74.36 O ANISOU 3465 O THR A 354 9530 8426 10297 -245 439 278 O ATOM 3466 CB THR A 354 227.384 6.713 77.029 1.00 74.22 C ANISOU 3466 CB THR A 354 9166 8873 10161 -321 455 -4 C ATOM 3467 OG1 THR A 354 226.515 6.935 75.914 1.00 72.15 O ANISOU 3467 OG1 THR A 354 8888 8661 9866 -398 513 52 O ATOM 3468 CG2 THR A 354 228.731 6.251 76.520 1.00 78.00 C ANISOU 3468 CG2 THR A 354 9464 9572 10601 -291 412 -216 C ATOM 3469 N ASN A 355 224.361 5.946 77.736 1.00 73.17 N ANISOU 3469 N ASN A 355 9289 8365 10148 -261 472 240 N ATOM 3470 CA ASN A 355 223.063 6.447 78.170 1.00 73.47 C ANISOU 3470 CA ASN A 355 9425 8308 10182 -293 521 375 C ATOM 3471 C ASN A 355 222.428 5.555 79.227 1.00 74.75 C ANISOU 3471 C ASN A 355 9684 8335 10384 -258 475 411 C ATOM 3472 O ASN A 355 221.718 6.058 80.106 1.00 73.45 O ANISOU 3472 O ASN A 355 9591 8118 10200 -283 506 496 O ATOM 3473 CB ASN A 355 222.130 6.590 76.970 1.00 73.43 C ANISOU 3473 CB ASN A 355 9381 8364 10156 -334 570 401 C ATOM 3474 CG ASN A 355 222.611 7.634 75.985 1.00 73.72 C ANISOU 3474 CG ASN A 355 9359 8526 10125 -418 602 403 C ATOM 3475 OD1 ASN A 355 223.774 8.036 76.007 1.00 73.18 O ANISOU 3475 OD1 ASN A 355 9249 8539 10018 -456 590 357 O ATOM 3476 ND2 ASN A 355 221.713 8.091 75.123 1.00 73.17 N ANISOU 3476 ND2 ASN A 355 9294 8479 10027 -464 632 459 N ATOM 3477 N ALA A 356 222.656 4.241 79.155 1.00 77.61 N ANISOU 3477 N ALA A 356 10054 8646 10789 -210 385 340 N ATOM 3478 CA ALA A 356 222.190 3.358 80.218 1.00 73.56 C ANISOU 3478 CA ALA A 356 9667 7990 10292 -218 305 388 C ATOM 3479 C ALA A 356 222.840 3.723 81.545 1.00 73.72 C ANISOU 3479 C ALA A 356 9756 7947 10307 -214 272 416 C ATOM 3480 O ALA A 356 222.201 3.650 82.601 1.00 76.00 O ANISOU 3480 O ALA A 356 10145 8166 10565 -275 266 504 O ATOM 3481 CB ALA A 356 222.474 1.900 79.859 1.00 71.62 C ANISOU 3481 CB ALA A 356 9449 7666 10096 -160 163 298 C ATOM 3482 N LEU A 357 224.112 4.124 81.508 1.00 70.52 N ANISOU 3482 N LEU A 357 9288 7591 9917 -157 254 336 N ATOM 3483 CA LEU A 357 224.753 4.658 82.703 1.00 63.57 C ANISOU 3483 CA LEU A 357 8461 6668 9027 -157 240 364 C ATOM 3484 C LEU A 357 224.188 6.023 83.071 1.00 61.12 C ANISOU 3484 C LEU A 357 8159 6397 8665 -222 359 464 C ATOM 3485 O LEU A 357 224.072 6.346 84.259 1.00 60.17 O ANISOU 3485 O LEU A 357 8116 6220 8526 -245 359 523 O ATOM 3486 CB LEU A 357 226.264 4.746 82.491 1.00 64.91 C ANISOU 3486 CB LEU A 357 8539 6913 9212 -86 191 235 C ATOM 3487 CG LEU A 357 226.994 3.414 82.312 1.00 66.77 C ANISOU 3487 CG LEU A 357 8761 7103 9506 27 29 89 C ATOM 3488 CD1 LEU A 357 228.417 3.649 81.845 1.00 70.73 C ANISOU 3488 CD1 LEU A 357 9107 7768 9999 97 9 -81 C ATOM 3489 CD2 LEU A 357 226.977 2.612 83.603 1.00 65.20 C ANISOU 3489 CD2 LEU A 357 8730 6704 9338 49 -114 133 C ATOM 3490 N ALA A 358 223.825 6.832 82.074 1.00 60.98 N ANISOU 3490 N ALA A 358 8073 6473 8622 -249 441 474 N ATOM 3491 CA ALA A 358 223.230 8.131 82.364 1.00 59.83 C ANISOU 3491 CA ALA A 358 7957 6340 8437 -285 509 550 C ATOM 3492 C ALA A 358 221.864 7.976 83.017 1.00 63.87 C ANISOU 3492 C ALA A 358 8522 6815 8932 -299 534 608 C ATOM 3493 O ALA A 358 221.533 8.709 83.955 1.00 63.85 O ANISOU 3493 O ALA A 358 8559 6800 8900 -303 554 641 O ATOM 3494 CB ALA A 358 223.125 8.957 81.083 1.00 60.17 C ANISOU 3494 CB ALA A 358 7944 6467 8451 -319 549 552 C ATOM 3495 N TYR A 359 221.058 7.026 82.538 1.00 71.22 N ANISOU 3495 N TYR A 359 9442 7751 9868 -315 531 607 N ATOM 3496 CA TYR A 359 219.747 6.794 83.137 1.00 74.57 C ANISOU 3496 CA TYR A 359 9896 8190 10248 -361 558 649 C ATOM 3497 C TYR A 359 219.863 6.146 84.509 1.00 74.80 C ANISOU 3497 C TYR A 359 10010 8161 10248 -415 506 679 C ATOM 3498 O TYR A 359 218.966 6.307 85.344 1.00 72.93 O ANISOU 3498 O TYR A 359 9788 7980 9943 -477 540 708 O ATOM 3499 CB TYR A 359 218.890 5.925 82.216 1.00 76.03 C ANISOU 3499 CB TYR A 359 10051 8405 10431 -390 563 645 C ATOM 3500 CG TYR A 359 218.391 6.642 80.983 1.00 75.57 C ANISOU 3500 CG TYR A 359 9916 8421 10377 -359 619 630 C ATOM 3501 CD1 TYR A 359 217.780 7.886 81.080 1.00 75.43 C ANISOU 3501 CD1 TYR A 359 9879 8450 10330 -330 660 636 C ATOM 3502 CD2 TYR A 359 218.531 6.076 79.721 1.00 78.22 C ANISOU 3502 CD2 TYR A 359 10204 8774 10743 -352 610 600 C ATOM 3503 CE1 TYR A 359 217.323 8.546 79.956 1.00 75.12 C ANISOU 3503 CE1 TYR A 359 9798 8452 10292 -304 675 628 C ATOM 3504 CE2 TYR A 359 218.075 6.729 78.591 1.00 78.55 C ANISOU 3504 CE2 TYR A 359 10187 8881 10777 -343 651 597 C ATOM 3505 CZ TYR A 359 217.473 7.964 78.716 1.00 76.48 C ANISOU 3505 CZ TYR A 359 9930 8644 10486 -323 676 619 C ATOM 3506 OH TYR A 359 217.018 8.620 77.595 1.00 77.19 O ANISOU 3506 OH TYR A 359 9989 8773 10566 -316 682 622 O ATOM 3507 N ALA A 360 220.952 5.414 84.758 1.00 75.90 N ANISOU 3507 N ALA A 360 10202 8205 10430 -397 413 661 N ATOM 3508 CA ALA A 360 221.120 4.754 86.048 1.00 76.58 C ANISOU 3508 CA ALA A 360 10399 8210 10487 -460 331 702 C ATOM 3509 C ALA A 360 221.185 5.757 87.190 1.00 77.03 C ANISOU 3509 C ALA A 360 10465 8302 10499 -476 383 728 C ATOM 3510 O ALA A 360 220.754 5.450 88.308 1.00 79.99 O ANISOU 3510 O ALA A 360 10911 8678 10804 -576 361 777 O ATOM 3511 CB ALA A 360 222.375 3.882 86.034 1.00 77.15 C ANISOU 3511 CB ALA A 360 10525 8162 10627 -396 190 651 C ATOM 3512 N SER A 361 221.711 6.959 86.934 1.00 74.75 N ANISOU 3512 N SER A 361 10115 8051 10237 -399 441 698 N ATOM 3513 CA SER A 361 221.759 7.975 87.980 1.00 72.97 C ANISOU 3513 CA SER A 361 9903 7849 9973 -402 478 712 C ATOM 3514 C SER A 361 220.361 8.370 88.434 1.00 74.29 C ANISOU 3514 C SER A 361 10042 8124 10062 -448 544 716 C ATOM 3515 O SER A 361 220.171 8.751 89.594 1.00 73.20 O ANISOU 3515 O SER A 361 9921 8027 9865 -483 557 719 O ATOM 3516 CB SER A 361 222.519 9.208 87.494 1.00 72.95 C ANISOU 3516 CB SER A 361 9861 7853 10003 -329 505 684 C ATOM 3517 OG SER A 361 221.757 9.930 86.545 1.00 73.95 O ANISOU 3517 OG SER A 361 9937 8037 10126 -304 553 673 O ATOM 3518 N SER A 362 219.374 8.283 87.540 1.00 76.49 N ANISOU 3518 N SER A 362 10260 8473 10331 -446 585 701 N ATOM 3519 CA SER A 362 217.996 8.566 87.924 1.00 78.67 C ANISOU 3519 CA SER A 362 10479 8892 10521 -483 641 672 C ATOM 3520 C SER A 362 217.424 7.498 88.847 1.00 77.17 C ANISOU 3520 C SER A 362 10326 8763 10230 -643 627 709 C ATOM 3521 O SER A 362 216.438 7.762 89.543 1.00 76.08 O ANISOU 3521 O SER A 362 10129 8793 9986 -706 676 671 O ATOM 3522 CB SER A 362 217.119 8.700 86.681 1.00 80.26 C ANISOU 3522 CB SER A 362 10604 9156 10736 -439 676 640 C ATOM 3523 OG SER A 362 217.113 7.495 85.939 1.00 78.23 O ANISOU 3523 OG SER A 362 10366 8857 10499 -498 653 677 O ATOM 3524 N ALA A 363 218.014 6.301 88.861 1.00 77.45 N ANISOU 3524 N ALA A 363 10462 8678 10287 -719 544 773 N ATOM 3525 CA ALA A 363 217.605 5.249 89.781 1.00 76.54 C ANISOU 3525 CA ALA A 363 10436 8581 10065 -908 487 835 C ATOM 3526 C ALA A 363 218.553 5.088 90.959 1.00 73.11 C ANISOU 3526 C ALA A 363 10113 8045 9620 -951 406 879 C ATOM 3527 O ALA A 363 218.144 4.553 91.995 1.00 72.76 O ANISOU 3527 O ALA A 363 10141 8053 9453 -1134 369 933 O ATOM 3528 CB ALA A 363 217.490 3.910 89.043 1.00 77.98 C ANISOU 3528 CB ALA A 363 10698 8667 10266 -977 397 881 C ATOM 3529 N ILE A 364 219.800 5.537 90.825 1.00 73.31 N ANISOU 3529 N ILE A 364 10152 7945 9756 -808 375 857 N ATOM 3530 CA ILE A 364 220.756 5.414 91.919 1.00 75.56 C ANISOU 3530 CA ILE A 364 10537 8133 10039 -832 293 890 C ATOM 3531 C ILE A 364 220.574 6.544 92.924 1.00 79.89 C ANISOU 3531 C ILE A 364 11031 8800 10522 -840 381 868 C ATOM 3532 O ILE A 364 220.648 6.327 94.139 1.00 81.74 O ANISOU 3532 O ILE A 364 11337 9047 10672 -957 342 910 O ATOM 3533 CB ILE A 364 222.192 5.369 91.360 1.00 75.29 C ANISOU 3533 CB ILE A 364 10519 7950 10137 -680 218 852 C ATOM 3534 CG1 ILE A 364 222.431 4.063 90.601 1.00 73.33 C ANISOU 3534 CG1 ILE A 364 10339 7579 9944 -670 88 848 C ATOM 3535 CG2 ILE A 364 223.213 5.522 92.476 1.00 77.30 C ANISOU 3535 CG2 ILE A 364 10848 8128 10395 -674 150 865 C ATOM 3536 CD1 ILE A 364 223.716 4.050 89.804 1.00 72.56 C ANISOU 3536 CD1 ILE A 364 10196 7409 9964 -503 32 758 C ATOM 3537 N ASN A 365 220.318 7.758 92.436 1.00 80.81 N ANISOU 3537 N ASN A 365 11033 9002 10670 -719 482 799 N ATOM 3538 CA ASN A 365 220.218 8.909 93.330 1.00 80.62 C ANISOU 3538 CA ASN A 365 10962 9069 10600 -688 539 753 C ATOM 3539 C ASN A 365 219.154 8.759 94.414 1.00 80.53 C ANISOU 3539 C ASN A 365 10920 9246 10433 -838 577 740 C ATOM 3540 O ASN A 365 219.443 9.119 95.568 1.00 79.61 O ANISOU 3540 O ASN A 365 10824 9166 10259 -879 574 735 O ATOM 3541 CB ASN A 365 219.985 10.184 92.509 1.00 84.77 C ANISOU 3541 CB ASN A 365 11398 9629 11182 -533 596 677 C ATOM 3542 CG ASN A 365 221.226 10.624 91.753 1.00 84.50 C ANISOU 3542 CG ASN A 365 11396 9449 11260 -429 561 690 C ATOM 3543 OD1 ASN A 365 222.335 10.160 92.028 1.00 82.04 O ANISOU 3543 OD1 ASN A 365 11148 9038 10986 -444 507 727 O ATOM 3544 ND2 ASN A 365 221.045 11.526 90.796 1.00 90.08 N ANISOU 3544 ND2 ASN A 365 12059 10159 12008 -336 580 653 N ATOM 3545 N PRO A 366 217.942 8.257 94.145 1.00 81.48 N ANISOU 3545 N PRO A 366 10979 9517 10462 -938 614 725 N ATOM 3546 CA PRO A 366 216.989 8.060 95.251 1.00 80.66 C ANISOU 3546 CA PRO A 366 10830 9647 10172 -1126 650 702 C ATOM 3547 C PRO A 366 217.478 7.086 96.309 1.00 80.39 C ANISOU 3547 C PRO A 366 10946 9550 10051 -1339 562 817 C ATOM 3548 O PRO A 366 216.926 7.072 97.415 1.00 80.24 O ANISOU 3548 O PRO A 366 10898 9729 9861 -1514 588 803 O ATOM 3549 CB PRO A 366 215.726 7.541 94.547 1.00 82.86 C ANISOU 3549 CB PRO A 366 11024 10085 10373 -1209 694 675 C ATOM 3550 CG PRO A 366 216.194 7.040 93.228 1.00 81.72 C ANISOU 3550 CG PRO A 366 10945 9730 10376 -1114 647 733 C ATOM 3551 CD PRO A 366 217.324 7.942 92.846 1.00 81.92 C ANISOU 3551 CD PRO A 366 10985 9580 10560 -898 634 712 C ATOM 3552 N ILE A 367 218.493 6.280 96.015 1.00 79.65 N ANISOU 3552 N ILE A 367 11008 9197 10058 -1329 443 916 N ATOM 3553 CA ILE A 367 219.052 5.367 97.006 1.00 79.97 C ANISOU 3553 CA ILE A 367 11225 9130 10031 -1508 312 1025 C ATOM 3554 C ILE A 367 220.171 6.028 97.799 1.00 82.28 C ANISOU 3554 C ILE A 367 11553 9329 10382 -1411 290 1017 C ATOM 3555 O ILE A 367 220.204 5.953 99.029 1.00 81.34 O ANISOU 3555 O ILE A 367 11490 9272 10142 -1566 262 1056 O ATOM 3556 CB ILE A 367 219.538 4.073 96.319 1.00 78.13 C ANISOU 3556 CB ILE A 367 11154 8656 9875 -1529 150 1109 C ATOM 3557 CG1 ILE A 367 218.365 3.331 95.677 1.00 76.50 C ANISOU 3557 CG1 ILE A 367 10934 8547 9584 -1672 161 1132 C ATOM 3558 CG2 ILE A 367 220.251 3.176 97.319 1.00 81.22 C ANISOU 3558 CG2 ILE A 367 11760 8880 10219 -1677 -37 1215 C ATOM 3559 CD1 ILE A 367 218.776 2.092 94.910 1.00 75.29 C ANISOU 3559 CD1 ILE A 367 10938 8153 9515 -1671 -11 1195 C ATOM 3560 N LEU A 368 221.103 6.691 97.111 1.00 84.58 N ANISOU 3560 N LEU A 368 11808 9486 10840 -1175 303 969 N ATOM 3561 CA LEU A 368 222.229 7.320 97.796 1.00 82.23 C ANISOU 3561 CA LEU A 368 11543 9103 10598 -1086 279 960 C ATOM 3562 C LEU A 368 221.770 8.494 98.653 1.00 85.36 C ANISOU 3562 C LEU A 368 11836 9685 10910 -1087 391 892 C ATOM 3563 O LEU A 368 221.985 8.515 99.870 1.00 87.53 O ANISOU 3563 O LEU A 368 12161 9997 11098 -1194 367 918 O ATOM 3564 CB LEU A 368 223.276 7.779 96.778 1.00 79.85 C ANISOU 3564 CB LEU A 368 11210 8663 10465 -869 272 916 C ATOM 3565 CG LEU A 368 224.084 6.696 96.063 1.00 76.74 C ANISOU 3565 CG LEU A 368 10901 8089 10167 -823 139 939 C ATOM 3566 CD1 LEU A 368 225.061 7.329 95.086 1.00 75.50 C ANISOU 3566 CD1 LEU A 368 10665 7884 10137 -636 163 867 C ATOM 3567 CD2 LEU A 368 224.817 5.819 97.065 1.00 78.43 C ANISOU 3567 CD2 LEU A 368 11275 8167 10358 -905 -25 1000 C ATOM 3568 N TYR A 369 221.125 9.482 98.031 1.00 82.26 N ANISOU 3568 N TYR A 369 11307 9408 10542 -962 496 794 N ATOM 3569 CA TYR A 369 220.788 10.717 98.727 1.00 80.39 C ANISOU 3569 CA TYR A 369 10972 9318 10253 -901 569 693 C ATOM 3570 C TYR A 369 219.677 10.543 99.754 1.00 89.21 C ANISOU 3570 C TYR A 369 12018 10700 11177 -1079 618 648 C ATOM 3571 O TYR A 369 219.418 11.478 100.519 1.00 93.31 O ANISOU 3571 O TYR A 369 12450 11367 11635 -1037 665 541 O ATOM 3572 CB TYR A 369 220.415 11.791 97.708 1.00 73.95 C ANISOU 3572 CB TYR A 369 10058 8518 9522 -705 618 593 C ATOM 3573 CG TYR A 369 221.552 12.096 96.764 1.00 73.84 C ANISOU 3573 CG TYR A 369 10105 8289 9662 -572 576 634 C ATOM 3574 CD1 TYR A 369 222.491 13.071 97.069 1.00 75.82 C ANISOU 3574 CD1 TYR A 369 10389 8452 9967 -480 555 618 C ATOM 3575 CD2 TYR A 369 221.705 11.388 95.582 1.00 76.64 C ANISOU 3575 CD2 TYR A 369 10477 8552 10089 -560 554 682 C ATOM 3576 CE1 TYR A 369 223.540 13.345 96.215 1.00 78.13 C ANISOU 3576 CE1 TYR A 369 10724 8596 10366 -401 520 651 C ATOM 3577 CE2 TYR A 369 222.749 11.653 94.723 1.00 79.09 C ANISOU 3577 CE2 TYR A 369 10817 8722 10510 -464 522 699 C ATOM 3578 CZ TYR A 369 223.665 12.632 95.044 1.00 79.53 C ANISOU 3578 CZ TYR A 369 10899 8719 10602 -397 507 685 C ATOM 3579 OH TYR A 369 224.706 12.895 94.188 1.00 77.93 O ANISOU 3579 OH TYR A 369 10711 8423 10476 -343 479 698 O ATOM 3580 N ASN A 370 219.018 9.387 99.792 1.00 93.95 N ANISOU 3580 N ASN A 370 12650 11379 11666 -1288 598 715 N ATOM 3581 CA ASN A 370 218.118 9.050 100.886 1.00100.68 C ANISOU 3581 CA ASN A 370 13454 12505 12294 -1535 630 697 C ATOM 3582 C ASN A 370 218.820 8.268 101.987 1.00103.39 C ANISOU 3582 C ASN A 370 13968 12760 12555 -1747 530 832 C ATOM 3583 O ASN A 370 218.159 7.791 102.915 1.00109.00 O ANISOU 3583 O ASN A 370 14677 13687 13052 -2020 533 854 O ATOM 3584 CB ASN A 370 216.911 8.267 100.366 1.00101.54 C ANISOU 3584 CB ASN A 370 13506 12788 12287 -1695 657 698 C ATOM 3585 CG ASN A 370 215.940 9.142 99.598 1.00102.12 C ANISOU 3585 CG ASN A 370 13373 13047 12382 -1517 761 526 C ATOM 3586 OD1 ASN A 370 215.162 9.891 100.189 1.00105.32 O ANISOU 3586 OD1 ASN A 370 13607 13742 12669 -1505 836 364 O ATOM 3587 ND2 ASN A 370 215.987 9.060 98.274 1.00 98.05 N ANISOU 3587 ND2 ASN A 370 12870 12372 12014 -1367 751 544 N ATOM 3588 N LEU A 371 220.141 8.120 101.895 1.00102.12 N ANISOU 3588 N LEU A 371 13953 12302 12547 -1639 433 916 N ATOM 3589 CA LEU A 371 220.960 7.596 102.980 1.00102.85 C ANISOU 3589 CA LEU A 371 14208 12283 12588 -1781 320 1023 C ATOM 3590 C LEU A 371 221.794 8.692 103.633 1.00105.32 C ANISOU 3590 C LEU A 371 14484 12568 12963 -1631 356 962 C ATOM 3591 O LEU A 371 222.800 8.397 104.286 1.00106.90 O ANISOU 3591 O LEU A 371 14821 12608 13188 -1662 253 1041 O ATOM 3592 CB LEU A 371 221.865 6.471 102.476 1.00102.69 C ANISOU 3592 CB LEU A 371 14387 11949 12682 -1773 144 1145 C ATOM 3593 CG LEU A 371 221.169 5.205 101.978 1.00100.49 C ANISOU 3593 CG LEU A 371 14206 11644 12334 -1955 55 1230 C ATOM 3594 CD1 LEU A 371 222.189 4.220 101.422 1.00 98.58 C ANISOU 3594 CD1 LEU A 371 14152 11068 12237 -1873 -146 1306 C ATOM 3595 CD2 LEU A 371 220.347 4.572 103.091 1.00100.23 C ANISOU 3595 CD2 LEU A 371 14244 11797 12041 -2322 17 1311 C ATOM 3596 N VAL A 372 221.398 9.949 103.460 1.00106.09 N ANISOU 3596 N VAL A 372 14413 12810 13088 -1463 480 818 N ATOM 3597 CA VAL A 372 222.118 11.076 104.037 1.00103.32 C ANISOU 3597 CA VAL A 372 14033 12431 12792 -1319 505 752 C ATOM 3598 C VAL A 372 221.227 11.812 105.033 1.00105.02 C ANISOU 3598 C VAL A 372 14106 12955 12843 -1385 594 619 C ATOM 3599 O VAL A 372 221.387 11.675 106.247 1.00103.67 O ANISOU 3599 O VAL A 372 13968 12876 12545 -1546 579 645 O ATOM 3600 CB VAL A 372 222.622 12.036 102.942 1.00103.71 C ANISOU 3600 CB VAL A 372 14040 12336 13030 -1043 528 689 C ATOM 3601 CG1 VAL A 372 223.294 13.250 103.567 1.00105.09 C ANISOU 3601 CG1 VAL A 372 14199 12486 13242 -919 540 622 C ATOM 3602 CG2 VAL A 372 223.575 11.316 102.001 1.00 99.10 C ANISOU 3602 CG2 VAL A 372 13565 11501 12587 -987 446 789 C TER 3603 VAL A 372 ATOM 3604 N ARG B 8 231.741 8.420 57.496 1.00 85.19 N ANISOU 3604 N ARG B 8 8119 15220 9030 -3265 1048 -1290 N ATOM 3605 CA ARG B 8 230.453 9.090 57.630 1.00 83.83 C ANISOU 3605 CA ARG B 8 8326 14549 8977 -3291 999 -910 C ATOM 3606 C ARG B 8 230.180 9.456 59.084 1.00 85.90 C ANISOU 3606 C ARG B 8 8849 14334 9455 -3073 946 -731 C ATOM 3607 O ARG B 8 230.006 8.580 59.929 1.00 87.68 O ANISOU 3607 O ARG B 8 9058 14327 9930 -2686 940 -841 O ATOM 3608 CB ARG B 8 229.331 8.206 57.084 1.00 81.76 C ANISOU 3608 CB ARG B 8 8075 14096 8892 -3058 1008 -926 C ATOM 3609 CG ARG B 8 229.490 6.728 57.405 1.00 84.71 C ANISOU 3609 CG ARG B 8 8237 14476 9472 -2638 1018 -1242 C ATOM 3610 CD ARG B 8 228.207 5.963 57.122 1.00 87.31 C ANISOU 3610 CD ARG B 8 8670 14495 10009 -2403 1007 -1183 C ATOM 3611 NE ARG B 8 228.371 4.524 57.303 1.00 89.80 N ANISOU 3611 NE ARG B 8 8803 14819 10498 -2037 983 -1487 N ATOM 3612 CZ ARG B 8 227.401 3.636 57.117 1.00 87.44 C ANISOU 3612 CZ ARG B 8 8563 14279 10382 -1807 959 -1492 C ATOM 3613 NH1 ARG B 8 226.195 4.039 56.744 1.00 80.90 N ANISOU 3613 NH1 ARG B 8 7942 13209 9586 -1897 976 -1223 N ATOM 3614 NH2 ARG B 8 227.635 2.344 57.302 1.00 92.15 N ANISOU 3614 NH2 ARG B 8 9019 14871 11123 -1488 900 -1773 N ATOM 3615 N ARG B 9 230.152 10.753 59.371 1.00 84.47 N ANISOU 3615 N ARG B 9 8918 14011 9167 -3336 890 -458 N ATOM 3616 CA ARG B 9 229.901 11.196 60.733 1.00 81.43 C ANISOU 3616 CA ARG B 9 8775 13197 8966 -3150 837 -294 C ATOM 3617 C ARG B 9 228.494 10.788 61.162 1.00 72.39 C ANISOU 3617 C ARG B 9 7829 11570 8107 -2824 811 -164 C ATOM 3618 O ARG B 9 227.571 10.780 60.339 1.00 72.34 O ANISOU 3618 O ARG B 9 7895 11489 8103 -2870 800 -66 O ATOM 3619 CB ARG B 9 230.064 12.712 60.857 1.00 85.75 C ANISOU 3619 CB ARG B 9 9576 13668 9338 -3503 752 -26 C ATOM 3620 CG ARG B 9 231.415 13.146 61.398 1.00 88.38 C ANISOU 3620 CG ARG B 9 9806 14265 9510 -3674 762 -115 C ATOM 3621 CD ARG B 9 231.287 14.322 62.357 1.00 92.74 C ANISOU 3621 CD ARG B 9 10685 14462 10090 -3745 660 147 C ATOM 3622 NE ARG B 9 230.538 15.428 61.773 1.00 96.75 N ANISOU 3622 NE ARG B 9 11501 14768 10492 -4020 536 441 N ATOM 3623 CZ ARG B 9 231.056 16.312 60.927 1.00103.06 C ANISOU 3623 CZ ARG B 9 12353 15830 10974 -4504 471 545 C ATOM 3624 NH1 ARG B 9 232.331 16.227 60.578 1.00105.28 N ANISOU 3624 NH1 ARG B 9 12370 16630 11000 -4778 545 368 N ATOM 3625 NH2 ARG B 9 230.303 17.288 60.439 1.00105.37 N ANISOU 3625 NH2 ARG B 9 12968 15876 11194 -4723 315 819 N ATOM 3626 N PRO B 10 228.298 10.429 62.428 1.00 68.97 N ANISOU 3626 N PRO B 10 7476 10829 7901 -2507 801 -167 N ATOM 3627 CA PRO B 10 226.945 10.133 62.907 1.00 68.27 C ANISOU 3627 CA PRO B 10 7577 10315 8050 -2242 777 -35 C ATOM 3628 C PRO B 10 226.066 11.374 62.873 1.00 70.99 C ANISOU 3628 C PRO B 10 8214 10392 8366 -2388 696 254 C ATOM 3629 O PRO B 10 226.543 12.511 62.843 1.00 76.70 O ANISOU 3629 O PRO B 10 9056 11158 8928 -2653 634 380 O ATOM 3630 CB PRO B 10 227.173 9.649 64.345 1.00 67.03 C ANISOU 3630 CB PRO B 10 7439 9950 8079 -1954 773 -99 C ATOM 3631 CG PRO B 10 228.607 9.229 64.385 1.00 67.73 C ANISOU 3631 CG PRO B 10 7280 10387 8069 -1982 802 -344 C ATOM 3632 CD PRO B 10 229.319 10.154 63.451 1.00 67.44 C ANISOU 3632 CD PRO B 10 7177 10699 7749 -2376 812 -318 C ATOM 3633 N TYR B 11 224.753 11.137 62.862 1.00 69.57 N ANISOU 3633 N TYR B 11 8156 9935 8341 -2211 679 347 N ATOM 3634 CA TYR B 11 223.771 12.208 62.926 1.00 69.17 C ANISOU 3634 CA TYR B 11 8379 9598 8305 -2264 577 582 C ATOM 3635 C TYR B 11 222.987 12.217 64.228 1.00 72.01 C ANISOU 3635 C TYR B 11 8883 9603 8874 -1978 553 644 C ATOM 3636 O TYR B 11 222.233 13.166 64.473 1.00 74.40 O ANISOU 3636 O TYR B 11 9405 9664 9199 -1980 450 804 O ATOM 3637 CB TYR B 11 222.793 12.111 61.744 1.00 66.86 C ANISOU 3637 CB TYR B 11 8110 9308 7987 -2323 559 640 C ATOM 3638 CG TYR B 11 222.141 10.755 61.593 1.00 64.35 C ANISOU 3638 CG TYR B 11 7643 8984 7823 -2074 648 507 C ATOM 3639 CD1 TYR B 11 222.740 9.760 60.835 1.00 64.62 C ANISOU 3639 CD1 TYR B 11 7428 9323 7801 -2099 732 312 C ATOM 3640 CD2 TYR B 11 220.929 10.469 62.209 1.00 63.99 C ANISOU 3640 CD2 TYR B 11 7703 8646 7965 -1822 638 563 C ATOM 3641 CE1 TYR B 11 222.154 8.521 60.693 1.00 64.96 C ANISOU 3641 CE1 TYR B 11 7362 9335 7983 -1877 785 193 C ATOM 3642 CE2 TYR B 11 220.335 9.230 62.073 1.00 64.22 C ANISOU 3642 CE2 TYR B 11 7616 8669 8116 -1631 707 456 C ATOM 3643 CZ TYR B 11 220.954 8.261 61.313 1.00 64.85 C ANISOU 3643 CZ TYR B 11 7481 9012 8149 -1658 771 279 C ATOM 3644 OH TYR B 11 220.377 7.024 61.167 1.00 65.99 O ANISOU 3644 OH TYR B 11 7534 9126 8411 -1473 812 173 O ATOM 3645 N ILE B 12 223.151 11.200 65.065 1.00 68.23 N ANISOU 3645 N ILE B 12 8290 9096 8538 -1740 627 511 N ATOM 3646 CA ILE B 12 222.432 11.096 66.328 1.00 64.89 C ANISOU 3646 CA ILE B 12 7981 8383 8289 -1497 615 556 C ATOM 3647 C ILE B 12 223.307 11.672 67.433 1.00 67.37 C ANISOU 3647 C ILE B 12 8352 8652 8594 -1506 591 570 C ATOM 3648 O ILE B 12 224.406 11.171 67.693 1.00 68.04 O ANISOU 3648 O ILE B 12 8296 8904 8653 -1508 634 439 O ATOM 3649 CB ILE B 12 222.055 9.639 66.625 1.00 64.75 C ANISOU 3649 CB ILE B 12 7844 8340 8417 -1267 682 428 C ATOM 3650 CG1 ILE B 12 221.079 9.122 65.566 1.00 64.52 C ANISOU 3650 CG1 ILE B 12 7777 8336 8401 -1259 701 429 C ATOM 3651 CG2 ILE B 12 221.488 9.515 68.030 1.00 64.39 C ANISOU 3651 CG2 ILE B 12 7905 8047 8514 -1069 673 469 C ATOM 3652 CD1 ILE B 12 220.754 7.652 65.693 1.00 65.77 C ANISOU 3652 CD1 ILE B 12 7830 8481 8679 -1073 745 303 C ATOM 3653 N LEU B 13 222.822 12.723 68.084 1.00 73.83 N ANISOU 3653 N LEU B 13 9371 9248 9432 -1497 510 709 N ATOM 3654 CA LEU B 13 223.550 13.332 69.190 1.00 80.34 C ANISOU 3654 CA LEU B 13 10269 10001 10254 -1498 480 732 C ATOM 3655 C LEU B 13 223.011 12.841 70.532 1.00 86.79 C ANISOU 3655 C LEU B 13 11114 10623 11241 -1237 507 707 C ATOM 3656 O LEU B 13 223.750 12.712 71.510 1.00 87.39 O ANISOU 3656 O LEU B 13 11168 10691 11345 -1182 526 661 O ATOM 3657 CB LEU B 13 223.465 14.857 69.110 1.00 77.48 C ANISOU 3657 CB LEU B 13 10127 9517 9795 -1664 345 891 C ATOM 3658 CG LEU B 13 224.188 15.631 70.212 1.00 75.60 C ANISOU 3658 CG LEU B 13 9991 9191 9542 -1685 295 928 C ATOM 3659 CD1 LEU B 13 225.677 15.340 70.171 1.00 73.53 C ANISOU 3659 CD1 LEU B 13 9573 9198 9169 -1837 364 834 C ATOM 3660 CD2 LEU B 13 223.927 17.119 70.079 1.00 75.39 C ANISOU 3660 CD2 LEU B 13 10221 8993 9432 -1831 119 1086 C ATOM 3661 OXT LEU B 13 221.820 12.557 70.669 1.00 90.26 O ANISOU 3661 OXT LEU B 13 11593 10925 11776 -1091 509 729 O TER 3662 LEU B 13 HETATM 3663 O16 TCE A1201 258.658 29.759 128.838 1.00 81.15 O ANISOU 3663 O16 TCE A1201 12074 9239 9521 -1650 -457 560 O HETATM 3664 C14 TCE A1201 257.721 30.597 128.759 1.00 81.54 C ANISOU 3664 C14 TCE A1201 12237 9175 9570 -1688 -406 601 C HETATM 3665 O15 TCE A1201 257.824 31.711 129.336 1.00 86.50 O ANISOU 3665 O15 TCE A1201 12959 9769 10138 -1779 -398 611 O HETATM 3666 C5 TCE A1201 256.460 30.261 127.966 1.00 80.56 C ANISOU 3666 C5 TCE A1201 12136 8955 9520 -1611 -371 623 C HETATM 3667 C2 TCE A1201 255.805 31.547 127.468 1.00 83.16 C ANISOU 3667 C2 TCE A1201 12577 9192 9827 -1675 -343 635 C HETATM 3668 P TCE A1201 254.101 31.160 126.822 1.00 81.34 P ANISOU 3668 P TCE A1201 12377 8843 9684 -1557 -305 646 P HETATM 3669 C3 TCE A1201 253.560 29.454 127.339 1.00 84.63 C ANISOU 3669 C3 TCE A1201 12718 9277 10162 -1442 -300 663 C HETATM 3670 C6 TCE A1201 252.196 29.480 128.032 1.00 83.51 C ANISOU 3670 C6 TCE A1201 12634 9074 10021 -1402 -265 663 C HETATM 3671 C8 TCE A1201 251.643 30.902 128.126 1.00 84.62 C ANISOU 3671 C8 TCE A1201 12863 9154 10135 -1415 -250 616 C HETATM 3672 O10 TCE A1201 250.899 31.349 127.215 1.00 87.06 O ANISOU 3672 O10 TCE A1201 13201 9399 10478 -1375 -244 595 O HETATM 3673 O9 TCE A1201 251.921 31.629 129.118 1.00 83.67 O ANISOU 3673 O9 TCE A1201 12794 9036 9959 -1455 -264 590 O HETATM 3674 C1 TCE A1201 254.061 31.312 124.971 1.00 81.21 C ANISOU 3674 C1 TCE A1201 12332 8836 9687 -1591 -301 653 C HETATM 3675 C4 TCE A1201 252.659 31.753 124.568 1.00 80.25 C ANISOU 3675 C4 TCE A1201 12301 8580 9611 -1527 -291 654 C HETATM 3676 C11 TCE A1201 252.509 33.254 124.810 1.00 84.41 C ANISOU 3676 C11 TCE A1201 12984 8997 10090 -1591 -347 642 C HETATM 3677 O12 TCE A1201 251.598 33.680 125.569 1.00 84.85 O ANISOU 3677 O12 TCE A1201 13109 8968 10161 -1508 -356 596 O HETATM 3678 O13 TCE A1201 253.298 34.065 124.256 1.00 88.82 O ANISOU 3678 O13 TCE A1201 13605 9561 10583 -1734 -398 667 O HETATM 3679 C1 GOL A1202 215.100 28.444 65.446 1.00101.40 C ANISOU 3679 C1 GOL A1202 16535 9399 12596 -1650 -3153 1941 C HETATM 3680 O1 GOL A1202 213.766 28.546 65.894 1.00102.09 O ANISOU 3680 O1 GOL A1202 16586 9332 12872 -1183 -3276 1740 O HETATM 3681 C2 GOL A1202 215.150 28.461 63.920 1.00101.97 C ANISOU 3681 C2 GOL A1202 16729 9518 12497 -2002 -3254 2117 C HETATM 3682 O2 GOL A1202 213.997 29.089 63.406 1.00100.77 O ANISOU 3682 O2 GOL A1202 16800 9085 12402 -1810 -3611 2092 O HETATM 3683 C3 GOL A1202 216.386 29.223 63.454 1.00106.50 C ANISOU 3683 C3 GOL A1202 17584 10059 12822 -2520 -3422 2355 C HETATM 3684 O3 GOL A1202 217.551 28.534 63.852 1.00106.56 O ANISOU 3684 O3 GOL A1202 17334 10394 12758 -2718 -3058 2359 O HETATM 3685 C1 PEG A1203 232.349 -3.242 66.917 1.00 94.27 C ANISOU 3685 C1 PEG A1203 9668 13492 12657 876 -360 -2932 C HETATM 3686 O1 PEG A1203 231.489 -3.697 65.908 1.00 95.11 O ANISOU 3686 O1 PEG A1203 9773 13592 12773 850 -334 -2920 O HETATM 3687 C2 PEG A1203 231.580 -3.072 68.227 1.00 93.20 C ANISOU 3687 C2 PEG A1203 9895 12865 12650 864 -384 -2576 C HETATM 3688 O2 PEG A1203 232.483 -2.813 69.267 1.00 89.58 O ANISOU 3688 O2 PEG A1203 9442 12391 12202 935 -450 -2626 O HETATM 3689 C3 PEG A1203 232.007 -1.942 70.256 1.00 83.53 C ANISOU 3689 C3 PEG A1203 8903 11389 11447 778 -343 -2275 C HETATM 3690 C4 PEG A1203 231.418 -2.740 71.419 1.00 79.12 C ANISOU 3690 C4 PEG A1203 8654 10345 11062 933 -527 -2140 C HETATM 3691 O4 PEG A1203 231.226 -1.899 72.523 1.00 77.75 O ANISOU 3691 O4 PEG A1203 8655 10000 10886 809 -441 -1866 O HETATM 3692 C1 PEG A1204 225.217 -11.200 66.131 1.00 95.59 C ANISOU 3692 C1 PEG A1204 11448 11192 13679 1520 -1568 -2529 C HETATM 3693 O1 PEG A1204 224.431 -12.118 65.420 1.00 95.75 O ANISOU 3693 O1 PEG A1204 11564 11080 13738 1541 -1683 -2556 O HETATM 3694 C2 PEG A1204 226.367 -10.721 65.247 1.00 93.70 C ANISOU 3694 C2 PEG A1204 10809 11426 13366 1622 -1463 -2861 C HETATM 3695 O2 PEG A1204 226.880 -9.518 65.746 1.00 91.83 O ANISOU 3695 O2 PEG A1204 10465 11379 13048 1495 -1251 -2749 O HETATM 3696 C3 PEG A1204 227.761 -9.674 66.823 1.00 88.61 C ANISOU 3696 C3 PEG A1204 10127 10843 12698 1648 -1432 -2842 C HETATM 3697 C4 PEG A1204 228.867 -8.622 66.742 1.00 84.81 C ANISOU 3697 C4 PEG A1204 9347 10772 12105 1610 -1252 -2972 C HETATM 3698 O4 PEG A1204 228.300 -7.341 66.747 1.00 81.89 O ANISOU 3698 O4 PEG A1204 8976 10506 11631 1310 -932 -2645 O HETATM 3699 C1 PEG A1205 206.437 5.438 70.809 1.00 73.79 C ANISOU 3699 C1 PEG A1205 8987 9131 9919 -381 893 445 C HETATM 3700 O1 PEG A1205 206.133 5.479 69.441 1.00 72.32 O ANISOU 3700 O1 PEG A1205 8774 8954 9750 -368 881 451 O HETATM 3701 C2 PEG A1205 205.945 6.718 71.483 1.00 79.70 C ANISOU 3701 C2 PEG A1205 9710 9927 10647 -258 851 374 C HETATM 3702 O2 PEG A1205 206.136 6.621 72.867 1.00 79.03 O ANISOU 3702 O2 PEG A1205 9633 9867 10527 -286 875 359 O HETATM 3703 C3 PEG A1205 205.193 7.319 73.632 1.00 81.07 C ANISOU 3703 C3 PEG A1205 9806 10274 10723 -204 864 246 C HETATM 3704 C4 PEG A1205 204.535 6.365 74.629 1.00 78.78 C ANISOU 3704 C4 PEG A1205 9443 10169 10320 -346 941 217 C HETATM 3705 O4 PEG A1205 204.675 6.858 75.934 1.00 77.97 O ANISOU 3705 O4 PEG A1205 9331 10118 10176 -325 939 165 O CONECT 703 1344 CONECT 1344 703 CONECT 3663 3664 CONECT 3664 3663 3665 3666 CONECT 3665 3664 CONECT 3666 3664 3667 CONECT 3667 3666 3668 CONECT 3668 3667 3669 3674 CONECT 3669 3668 3670 CONECT 3670 3669 3671 CONECT 3671 3670 3672 3673 CONECT 3672 3671 CONECT 3673 3671 CONECT 3674 3668 3675 CONECT 3675 3674 3676 CONECT 3676 3675 3677 3678 CONECT 3677 3676 CONECT 3678 3676 CONECT 3679 3680 3681 CONECT 3680 3679 CONECT 3681 3679 3682 3683 CONECT 3682 3681 CONECT 3683 3681 3684 CONECT 3684 3683 CONECT 3685 3686 3687 CONECT 3686 3685 CONECT 3687 3685 3688 CONECT 3688 3687 3689 CONECT 3689 3688 3690 CONECT 3690 3689 3691 CONECT 3691 3690 CONECT 3692 3693 3694 CONECT 3693 3692 CONECT 3694 3692 3695 CONECT 3695 3694 3696 CONECT 3696 3695 3697 CONECT 3697 3696 3698 CONECT 3698 3697 CONECT 3699 3700 3701 CONECT 3700 3699 CONECT 3701 3699 3702 CONECT 3702 3701 3703 CONECT 3703 3702 3704 CONECT 3704 3703 3705 CONECT 3705 3704 MASTER 341 0 5 22 5 0 5 6 3703 2 45 41 END